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O88093 (HBP_ECOLX) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Hemoglobin-binding protease hbp autotransporter
EC=3.4.21.-

Cleaved into the following 2 chains:

  1. Hemoglobin-binding protease hbp
  2. Hemoglobin-binding protease hbp translocator
    Alternative name(s):
    Helper peptide
Gene names
Name:hbp
Encoded onPlasmid IncFI ColV3-K30
OrganismEscherichia coli
Taxonomic identifier562 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length1377 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with hemoglobin, degrades it and subsequently binds the released heme. Could make heme accessible not only for E.coli, but also for B.fragilis during mixed intra-abdominal infections. Has a role in abscess formation. Ref.1 Ref.2

Enzyme regulation

Protease activity is inhibited by 3,4-dichloroisocoumarin.

Subcellular location

Hemoglobin-binding protease hbp autotransporter: Periplasm By similarity Ref.1.

Hemoglobin-binding protease hbp: Secreted. Cell surface Ref.1.

Hemoglobin-binding protease hbp translocator: Cell outer membrane; Multi-pass membrane protein By similarity. Note: The cleaved C-terminal fragment (autotransporter domain) is localized in the outer membrane By similarity.

Domain

The signal peptide, cleaved at the inner membrane, guides the autotransporter protein to the periplasmic space. Then, insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, with subsequent cleavage.

Post-translational modification

Cleaved to release the mature protein from the outer membrane.

Sequence similarities

Contains 1 autotransporter (TC 1.B.12) domain. [View classification]

Contains 1 peptidase S6 domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5252 Ref.1
Chain53 – 13771325Hemoglobin-binding protease hbp autotransporter
PRO_0000387597
Chain53 – 11001048Hemoglobin-binding protease hbp
PRO_0000041982
Chain1101 – 1377277Hemoglobin-binding protease hbp translocator
PRO_0000041983

Regions

Domain1111 – 1377267Autotransporter

Sites

Active site1251Charge relay system
Active site1531Charge relay system
Active site2591Charge relay system
Site1100 – 11012Cleavage

Secondary structure

1 .............................................................................................................................................................................................................. 1377
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O88093 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: BB16D898EDAC0416

FASTA1,377148,257
        10         20         30         40         50         60 
MNRIYSLRYS AVARGFIAVS EFARKCVHKS VRRLCFPVLL LIPVLFSAGS LAGTVNNELG 

        70         80         90        100        110        120 
YQLFRDFAEN KGMFRPGATN IAIYNKQGEF VGTLDKAAMP DFSAVDSEIG VATLINPQYI 

       130        140        150        160        170        180 
ASVKHNGGYT NVSFGDGENR YNIVDRNNAP SLDFHAPRLD KLVTEVAPTA VTAQGAVAGA 

       190        200        210        220        230        240 
YLDKERYPVF YRLGSGTQYI KDSNGQLTKM GGAYSWLTGG TVGSLSSYQN GEMISTSSGL 

       250        260        270        280        290        300 
VFDYKLNGAM PIYGEAGDSG SPLFAFDTVQ NKWVLVGVLT AGNGAGGRGN NWAVIPLDFI 

       310        320        330        340        350        360 
GQKFNEDNDA PVTFRTSEGG ALEWSFNSST GAGALTQGTT TYAMHGQQGN DLNAGKNLIF 

       370        380        390        400        410        420 
QGQNGQINLK DSVSQGAGSL TFRDNYTVTT SNGSTWTGAG IVVDNGVSVN WQVNGVKGDN 

       430        440        450        460        470        480 
LHKIGEGTLT VQGTGINEGG LKVGDGKVVL NQQADNKGQV QAFSSVNIAS GRPTVVLTDE 

       490        500        510        520        530        540 
RQVNPDTVSW GYRGGTLDVN GNSLTFHQLK AADYGAVLAN NVDKRATITL DYALRADKVA 

       550        560        570        580        590        600 
LNGWSESGKG TAGNLYKYNN PYTNTTDYFI LKQSTYGYFP TDQSSNATWE FVGHSQGDAQ 

       610        620        630        640        650        660 
KLVADRFNTA GYLFHGQLKG NLNVDNRLPE GVTGALVMDG AADISGTFTQ ENGRLTLQGH 

       670        680        690        700        710        720 
PVIHAYNTQS VADKLAASGD HSVLTQPTSF SQEDWENRSF TFDRLSLKNT DFGLGRNATL 

       730        740        750        760        770        780 
NTTIQADNSS VTLGDSRVFI DKNDGQGTAF TLEEGTSVAT KDADKSVFNG TVNLDNQSVL 

       790        800        810        820        830        840 
NINDIFNGGI QANNSTVNIS SDSAVLGNST LTSTALNLNK GANALASQSF VSDGPVNISD 

       850        860        870        880        890        900 
ATLSLNSRPD EVSHTLLPVY DYAGSWNLKG DDARLNVGPY SMLSGNINVQ DKGTVTLGGE 

       910        920        930        940        950        960 
GELSPDLTLQ NQMLYSLFNG YRNIWSGSLN APDATVSMTD TQWSMNGNST AGNMKLNRTI 

       970        980        990       1000       1010       1020 
VGFNGGTSPF TTLTTDNLDA VQSAFVMRTD LNKADKLVIN KSATGHDNSI WVNFLKKPSN 

      1030       1040       1050       1060       1070       1080 
KDTLDIPLVS APEATADNLF RASTRVVGFS DVTPILSVRK EDGKKEWVLD GYQVARNDGQ 

      1090       1100       1110       1120       1130       1140 
GKAAATFMHI SYNNFITEVN NLNKRMGDLR DINGEAGTWV RLLNGSGSAD GGFTDHYTLL 

      1150       1160       1170       1180       1190       1200 
QMGADRKHEL GSMDLFTGVM ATYTDTDASA DLYSGKTKSW GGGFYASGLF RSGAYFDVIA 

      1210       1220       1230       1240       1250       1260 
KYIHNENKYD LNFAGAGKQN FRSHSLYAGA EVGYRYHLTD TTFVEPQAEL VWGRLQGQTF 

      1270       1280       1290       1300       1310       1320 
NWNDSGMDVS MRRNSVNPLV GRTGVVSGKT FSGKDWSLTA RAGLHYEFDL TDSADVHLKD 

      1330       1340       1350       1360       1370 
AAGEHQINGR KDSRMLYGVG LNARFGDNTR LGLEVERSAF GKYNTDDAIN ANIRYSF

« Hide

References

[1]"Characterization of a hemoglobin protease secreted by the pathogenic Escherichia coli strain EB1."
Otto B.R., van Dooren S.J.M., Nuijens J.H., Luirink J., Oudega B.
J. Exp. Med. 188:1091-1103(1998) [PubMed: 9743528] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 53-66, FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: O8:K43 / EB1.
[2]"Escherichia coli hemoglobin protease autotransporter contributes to synergistic abscess formation and heme-dependent growth of Bacteroides fragilis."
Otto B.R., van Dooren S.J.M., Dozois C.M., Luirink J., Oudega B.
Infect. Immun. 70:5-10(2002) [PubMed: 11748157] [Abstract]
Cited for: FUNCTION.
Strain: O8:K43 / EB1.
[3]"Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein."
Sijbrandi R., Urbanus M.L., ten Hagen-Jongman C.M., Bernstein H.D., Oudega B., Otto B.R., Luirink J.
J. Biol. Chem. 278:4654-4659(2003) [PubMed: 12466262] [Abstract]
Cited for: SECRETION.
Strain: O8:K43 / EB1.
[4]"Crystal structure of hemoglobin protease, a heme binding autotransporter protein from pathogenic Escherichia coli."
Otto B.R., Sijbrandi R., Luirink J., Oudega B., Heddle J.G., Mizutani K., Park S.-Y., Tame J.R.H.
J. Biol. Chem. 280:17339-17345(2005) [PubMed: 15728184] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 53-1100.
Strain: O8:K43 / EB1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ223631 Genomic DNA. Translation: CAA11507.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXRX-ray2.20A53-1100[»]
3AEHX-ray2.00A/B1075-1377[»]
3AK5X-ray2.20A/B/C/D53-1100[»]
ProteinModelPortalO88093.
SMRO88093. Positions 1101-1377.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR005546. Auto_transptbeta.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR000710. Peptidase_S6.
[Graphical view]
Gene3DG3DSA:2.160.20.20. P22_tailspike. 2 hits.
PfamPF03797. Autotransporter. 1 hit.
PF02395. Peptidase_S6. 1 hit.
[Graphical view]
PRINTSPR00921. IGASERPTASE.
SMARTSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMSSF103515. Auto_transptbeta. 1 hit.
SSF51126. Pectin_lyas_like. 1 hit.
TIGRFAMsTIGR01414. Autotrans_barl. 1 hit.
PROSITEPS51208. AUTOTRANSPORTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHBP_ECOLX
AccessionPrimary (citable) accession number: O88093
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: November 1, 1998
Last modified: December 14, 2011
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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