SPRINT Home UMBER Home Contents Standard Search Advanced Search Relation Search

==SPRINT==> PRINTS View



  selected as


PR00601

Identifier
BACFERRITIN  [View Relations]  [View Alignment]  
Accession
PR00601
No. of Motifs
7
Creation Date
12-AUG-1996  (UPDATE 26-JUN-1999)
Title
Bacterioferritin signature
Database References

PROSITE; PS00549 BACTERIOFERRITIN
BLOCKS; BL00549
PFAM; PF01334 Bacteriofer
INTERPRO; IPR002024
PDB; 1BCF
SCOP; 1BCF
CATH; 1BCF
Literature References
1. HARRISON, P.M. AND AROSIO, P.
The ferritins: molecular properties, iron storage function and cellular 
regulation.
BIOCHIM.BIOPHYS.ACTA 1275 161-203 (1996).
 
2. LE BRUN, N.E., ANDREWS, S.C., GUEST, J.R., HARRISON, P.M., MOORE, G.R.
AND THOMSON, A.J.                                                        
Identification of the ferroxidase centre of Escherichia coli 
bacterioferritin. 
BIOCHEM.J. 312 385-392 (1995). 
 
3. FROLOW, F., KALB, A.J. AND YARIV, J.
Structure of a unique twofold symmetric haem-binding site.
NAT.STRUCT.BIOL. 1 453-460 (1994). 
 
4. ANDREWS, S.C., LE BRUN, N.E., BARYNIN, V., THOMSON, A.J., MOORE, G.R.,
GUEST, J.R. AND HARRISON, P.M. 
Site-directed replacement of the coaxial heme ligands of bacterioferritin 
generates heme-free variants. 
J.BIOL.CHEM. 270 23268-23274 (1995). 

Documentation
Bacterioferritin (BFR; also known as cytochrome b1 or cytochrome b557) of 
Escherichia coli is an iron-storage protein consisting of 24 identical
subunits that pack together to form a highly symmetrical, nearly spherical 
shell surrounding a central cavity of about 8 nm diameter [1,2]. X-ray 
crystallographic studies have revealed a close structural similarity 
between BFR and the ferritins, a family of iron-storage proteins found in 
both eukaryota and prokaryota [1]. Common to both ferritins and BFRs is a 
capacity to store large quantities of iron within their hollow interior, in
the form of a hydrated ferric oxide mineral containing variable amounts of
phosphate anion. However, a major difference between them is that BFR 
contains up 12 b-type haem groups, while ferritins, as isolated, do not 
contain haem. 
 
The building block for the BFR shell is a protein dimer (subunits A and B) 
binding the single haem group. Each subunit consists of four nearly 
parallel alpha-helices. The haem is bound symmetrically to subunits A and B
by Met(A)-52 and Met(B)-52 residues [3]. Each subunit includes a binuclear 
metal-binding site linking together the four major helices of the subunit, 
which has been identified as the ferroxidase centre of BFR [2]:
 
                                 Glu-127
                                 |
                       O         C         O
                       |        / \        |
               Glu-18--C--O    O   O    O--C--Glu-94
                           `M1'     `M2'
               His-54--+--N'  `O   O'  `N--+--His-130
                       |   \    \ /    /   |
                       |   /     C     \   |
                       +--N      |      N--+
                                 Glu-51
 
(M1 and M2 are the metal centres 1 and 2). BFR mutants with Met-52 replaced
are haem-free, but appear to be correctly assembled and are capable of 
accumulating iron [4]. 
 
BACFERRITIN is a 7-element fingerprint that provides a signature for the
BFRs. The fingerprint was derived from an initial alignment of 5 sequences:
the motifs were drawn from conserved regions spanning virtually the full 
alignment length - motifs 1 and 2 encompass helix A, motif 1 spanning the
region encoded by PROSITE pattern BACTERIOFERRITIN (PS00549), which includes
Glu-18, one of six residues that form the binuclear-metal centre; motif 3, 
which spans most of helix B, includes Met-52, which provides an axial haem 
iron ligand, and the Glu-51 and His-54 components of the metal centre; 
motif 4 spans the B-C connecting loop; motif 5 includes most of helix C; 
and motifs 6 and 7, which encompass helix D, contain invariant residues 
Glu-94, Glu-127 and His-130 res., which also contribute to the metal- 
binding site. Two iterations on OWL28.1 were required to reach convergence, 
at which point a true set comprising 6 sequences was identified. Four 
partial matches were also found, all of which are N-terminal BFR fragments.
 
An update on SPTR37_9f identified a true set of 13 sequences, and 3
partial matches.
Summary Information
  13 codes involving  7 elements
1 codes involving 6 elements
1 codes involving 5 elements
1 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
713131313131313
61110111
51110101
40110011
30000000
20000000
1234567
True Positives
BFRB_NEIGO    BFR_AZOVI     BFR_BRUME     BFR_ECOLI     
BFR_MYCAV BFR_MYCLE BFR_RHOCA BFR_SYNY3
O08465 O50172 O68926 O68935
P73287
True Positive Partials
Codes involving 6 elements
BFR_PSEPU
Codes involving 5 elements
O50171
Codes involving 4 elements
BFRA_NEIGO
Sequence Titles
BFRB_NEIGO  BACTERIOFERRITIN B (BFR A) (BFR B) - NEISSERIA GONORRHOEAE. 
BFR_AZOVI BACTERIOFERRITIN (BFR) (CYTOCHROME B-557.5) - AZOTOBACTER VINELANDII.
BFR_BRUME BACTERIOFERRITIN (BFR) - BRUCELLA MELITENSIS.
BFR_ECOLI BACTERIOFERRITIN (BFR) (CYTOCHROME B-1) (CYTOCHROME B-557) - ESCHERICHIA COLI.
BFR_MYCAV BACTERIOFERRITIN (BFR) - MYCOBACTERIUM AVIUM.
BFR_MYCLE BACTERIOFERRITIN (BFR) (MAJOR MEMBRANE PROTEIN II) (MMP-II) - MYCOBACTERIUM LEPRAE.
BFR_RHOCA BACTERIOFERRITIN (BFR) - RHODOBACTER CAPSULATUS (RHODOPSEUDOMONAS CAPSULATA).
BFR_SYNY3 BACTERIOFERRITIN (BFR) - SYNECHOCYSTIS SP. (STRAIN PCC 6803).
O08465 BACTERIOFERRITIN (BFR) - MYCOBACTERIUM TUBERCULOSIS.
O50172 BACTERIOFERRITIN SUBUNIT 2 - MAGNETOSPIRILLUM MAGNETOTACTICUM (AQUASPIRILLUM MAGNETOTACTICUM).
O68926 BACTERIOFERRITIN - SALMONELLA TYPHIMURIUM.
O68935 BACTERIOFERRITIN - SERRATIA MARCESCENS.
P73287 BACTERIOFERRITIN - SYNECHOCYSTIS SP. (STRAIN PCC 6803).

BFR_PSEPU BACTERIOFERRITIN (BFR) - PSEUDOMONAS PUTIDA.

O50171 BACTERIOFERRITIN SUBUNIT 1 - MAGNETOSPIRILLUM MAGNETOTACTICUM (AQUASPIRILLUM MAGNETOTACTICUM).

BFRA_NEIGO BACTERIOFERRITIN A - NEISSERIA GONORRHOEAE.
Scan History
OWL28_1    2  50   NSINGLE    
SPTR37_9f 3 17 NSINGLE
Initial Motifs
Motif 1  width=20
Element Seqn Id St Int Rpt
GDPEVLRLLNEQLTTQLTAI BFR_MYCAV 3 3 -
GDKIVIQHLNKILGNELIAI BFR_AZOVI 3 3 -
GDTKVINYLNKLLGNELVAI BFR_ECOLI 3 3 -
GDAKVIEFLNAALRSELTAI RCBFGN 3 3 -
GEPKVIERLNDALFLELGAV BMU19760 3 3 -

Motif 2 width=21
Element Seqn Id St Int Rpt
NQYFLHARMFKNWGLKRLNDV BFR_ECOLI 23 0 -
NQYWLHYRLLNDWGYTRLAKK BMU19760 23 0 -
SQYWVHFRLQEDWGLAKMAKK RCBFGN 23 0 -
NQYFLHARMYEDWGLEKLGKH BFR_AZOVI 23 0 -
NQYFLHSKMQDNWGFTELAEH BFR_MYCAV 23 0 -

Motif 3 width=21
Element Seqn Id St Int Rpt
EYHESIDEMKHADRYIERILF BFR_ECOLI 44 0 -
SREESIEEMGHADKIIARILF RCBFGN 44 0 -
EREESIEEMHHADKLINRIIF BMU19760 44 0 -
TRAESFDEMRHAEAITDRILL BFR_MYCAV 44 0 -
EYHESIDEMKHADKLIKRILF BFR_AZOVI 44 0 -

Motif 4 width=21
Element Seqn Id St Int Rpt
FEGFPNLQTVSPLRIGQNVKE BMU19760 65 0 -
LDGLPNYQRLFSLRIGQTLRE BFR_MYCAV 65 0 -
LEGLPNLQELGKLLIGEHTKE BFR_AZOVI 65 0 -
LEGLPNLQDLGKLNIGEDVEE BFR_ECOLI 65 0 -
LEGHPNLQKLDPLRIGEGPRE RCBFGN 65 0 -

Motif 5 width=21
Element Seqn Id St Int Rpt
TLECDLAGEHDALKLYREARD RCBFGN 86 0 -
MLRSDLALELDGAKNLREAIG BFR_ECOLI 86 0 -
MLECDLKLEQAGLPDLKAAIA BFR_AZOVI 86 0 -
QFEADLAIEYEVMDRLKPAII BFR_MYCAV 86 0 -
VLEADLKGEYDARASYKESRE BMU19760 86 0 -

Motif 6 width=21
Element Seqn Id St Int Rpt
YCAEVGDIVSKNIFESLITDE RCBFGN 107 0 -
LCREKQDSTTATLFEQIVADE BFR_MYCAV 107 0 -
ICDKLGDYVSKQLFDELLADE BMU19760 107 0 -
YADSVHDYVSRDMMIEILRDE BFR_ECOLI 107 0 -
YCESVGDYASRELLEDILESE BFR_AZOVI 107 0 -

Motif 7 width=22
Element Seqn Id St Int Rpt
EGHIDFLETQLDLLAKIGEERY BMU19760 128 0 -
EKHIDYLETQLELMDKLGVELY BFR_MYCAV 128 0 -
EGHIDWLETELDLIQKMGLQNY BFR_ECOLI 128 0 -
EDHIDWLETQLDLIDKIGLENY BFR_AZOVI 128 0 -
EGHVDFLETQISLYDRLGPQGF RCBFGN 128 0 -
Final Motifs
Motif 1  width=20
Element Seqn Id St Int Rpt
GDVKIINYLNKLLGNELVAI O68926 3 3 -
GDTKVINYLNKLLGNELVAI BFR_ECOLI 3 3 -
GDKKIIAHLNKLLGNELVAI O68935 3 3 -
GDKIVIQHLNKILGNELIAI BFR_AZOVI 3 3 -
GDKEVLRHLNGVLKLHLTAI O50172 3 3 -
GDPDVLRLLNEQLTSELTAI O08465 3 3 -
GDPDVLRLLNEQLTSELTAI BFR_MYCLE 3 3 -
GDPEVLRLLNEQLTTQLTAI BFR_MYCAV 3 3 -
GDRLVIRELNKNLGLLLVTI BFRB_NEIGO 3 3 -
GEPKVIERLNDALFLELGAV BFR_BRUME 3 3 -
GNLEVRQHLNQALKLQLTAI P73287 22 22 -
GDAKVIEFLNAALRSELTAI BFR_RHOCA 3 3 -
GKPAVLAQLHKLLRGELAAR BFR_SYNY3 3 3 -

Motif 2 width=21
Element Seqn Id St Int Rpt
NQYFLHARMFKNWGLTRLNDV O68926 23 0 -
NQYFLHARMFKNWGLKRLNDV BFR_ECOLI 23 0 -
NQYFLHARMFKNWGLMRLNDK O68935 23 0 -
NQYFLHARMYEDWGLEKLGKH BFR_AZOVI 23 0 -
NQYFLHARMLKNWGLKDLGKA O50172 23 0 -
NQYFLHSKMQDNWGFTELAAH O08465 23 0 -
NQYFLHSKMQENWGFTELAER BFR_MYCLE 23 0 -
NQYFLHSKMQDNWGFTELAEH BFR_MYCAV 23 0 -
NQYFLHARILKNWGFEELGEH BFRB_NEIGO 23 0 -
NQYWLHYRLLNDWGYTRLAKK BFR_BRUME 23 0 -
NQYFLHARMCKNWGLNALNQY P73287 42 0 -
SQYWVHFRLQEDWGLAKMAKK BFR_RHOCA 23 0 -
DQYFIHSRMYQDWGLEKLYSR BFR_SYNY3 23 0 -

Motif 3 width=21
Element Seqn Id St Int Rpt
EYHESIDEMKHADKYIERILF O68926 44 0 -
EYHESIDEMKHADRYIERILF BFR_ECOLI 44 0 -
EYHESIDEMKHADRYIERILF O68935 44 0 -
EYHESIDEMKHADKLIKRILF BFR_AZOVI 44 0 -
VYKYSIEEMKQADEVIERILF O50172 44 0 -
TRAESFDEMRHAEEITDRILL O08465 44 0 -
TRVESFDEMRHAEAITDRILL BFR_MYCLE 44 0 -
TRAESFDEMRHAEAITDRILL BFR_MYCAV 44 0 -
FFKQSIVEMKAADDLIERILF BFRB_NEIGO 44 0 -
EREESIEEMHHADKLINRIIF BFR_BRUME 44 0 -
EYKVSIKAMKQADSLIERVLF P73287 63 0 -
SREESIEEMGHADKIIARILF BFR_RHOCA 44 0 -
IDHEMQDETAHASLLIERILF BFR_SYNY3 44 0 -

Motif 4 width=21
Element Seqn Id St Int Rpt
LEGIPNLQDLGKLGIGEDVEE O68926 65 0 -
LEGLPNLQDLGKLNIGEDVEE BFR_ECOLI 65 0 -
LEGIPNLQDLGKLNIGEDIEE O68935 65 0 -
LEGLPNLQELGKLLIGEHTKE BFR_AZOVI 65 0 -
LEGLPNLQDLGKLGIGEDVAE O50172 65 0 -
LDGLPNYQRIGSLRIGQTLRE O08465 65 0 -
LDGLPNYQRIGSLRVGQTLRE BFR_MYCLE 65 0 -
LDGLPNYQRLFSLRIGQTLRE BFR_MYCAV 65 0 -
LEGLPNLQELGKLLIGESTEE BFRB_NEIGO 65 0 -
FEGFPNLQTVSPLRIGQNVKE BFR_BRUME 65 0 -
LEGLPNLQNLEKLLIGETVPE P73287 84 0 -
LEGHPNLQKLDPLRIGEGPRE BFR_RHOCA 65 0 -
LEETPDLSQQDPIRVGKTVPE BFR_SYNY3 65 0 -

Motif 5 width=21
Element Seqn Id St Int Rpt
MLRSDLRLELEGAKDLREAIA O68926 86 0 -
MLRSDLALELDGAKNLREAIG BFR_ECOLI 86 0 -
MLRSDLALELAGAKNLREGIA O68935 86 0 -
MLECDLKLEQAGLPDLKAAIA BFR_AZOVI 86 0 -
MLASDLKMEQAEHKALTEAIA O50172 86 0 -
QFEADLAIEYDVLNRLKPGIV O08465 86 0 -
QFEADLAIEYEVMSRLKPGII BFR_MYCLE 86 0 -
QFEADLAIEYEVMDRLKPAII BFR_MYCAV 86 0 -
IIACDLTKEQEKHEALLAAIA BFRB_NEIGO 86 0 -
VLEADLKGEYDARASYKESRE BFR_BRUME 86 0 -
ILGNDLTMNQGIRDGLVNSIA P73287 105 0 -
TLECDLAGEHDALKLYREARD BFR_RHOCA 86 0 -
MLQYDLDYEYEVIANLKEAMA BFR_SYNY3 86 0 -

Motif 6 width=21
Element Seqn Id St Int Rpt
YADSVHDYVSRDMMIEILADE O68926 107 0 -
YADSVHDYVSRDMMIEILRDE BFR_ECOLI 107 0 -
YADSIHDYVSRDLMIDILADE O68935 107 0 -
YCESVGDYASRELLEDILESE BFR_AZOVI 107 0 -
LCETKQDFVTRDELGEILEDT O50172 107 0 -
MCREKQDTTSAVLLEKIVADE O08465 107 0 -
MCREKQDSTSAVLLEKIVADE BFR_MYCLE 107 0 -
LCREKQDSTTATLFEQIVADE BFR_MYCAV 107 0 -
TAEAQQDYVSRDLLEKQKDTN BFRB_NEIGO 107 0 -
ICDKLGDYVSKQLFDELLADE BFR_BRUME 107 0 -
FFETQRDYVSRDVLSEILEET P73287 126 0 -
YCAEVGDIVSKNIFESLITDE BFR_RHOCA 107 0 -
VCEQEQDYQSRDLLLKILADT BFR_SYNY3 107 0 -

Motif 7 width=22
Element Seqn Id St Int Rpt
EGHIDWLETELDLIAKLGMQNY O68926 128 0 -
EGHIDWLETELDLIQKMGLQNY BFR_ECOLI 128 0 -
EEHIDWLETELDLIARLGIQNY O68935 128 0 -
EDHIDWLETQLDLIDKIGLENY BFR_AZOVI 128 0 -
EEHIDWLETQIDLMAKMGTQNY O50172 128 0 -
EEHIDYLETQLELMDKLGEELY O08465 128 0 -
EEHIDYLETQLALMGQLGEELY BFR_MYCLE 128 0 -
EKHIDYLETQLELMDKLGVELY BFR_MYCAV 128 0 -
EKHIDWLETQQELIGKIGLPNY BFRB_NEIGO 128 0 -
EGHIDFLETQLDLLAKIGEERY BFR_BRUME 128 0 -
EEQIDWLESQQWLISNSGLENY P73287 147 0 -
EGHVDFLETQISLYDRLGPQGF BFR_RHOCA 128 0 -
EDHAYWLEKQLGLIEKIGLQNY BFR_SYNY3 129 1 -