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Protein

Hemoglobin-binding protease hbp autotransporter

Gene

hbp

Organism
Escherichia coli
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Enzyme regulationi

Protease activity is inhibited by 3,4-dichloroisocoumarin.

pH dependencei

Optimum pH is 6.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei125 – 1251Charge relay system
Active sitei153 – 1531Charge relay system
Active sitei259 – 2591Charge relay system

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Virulence

Names & Taxonomyi

Protein namesi
Recommended name:
Hemoglobin-binding protease hbp autotransporter (EC:3.4.21.-)
Cleaved into the following 2 chains:
Gene namesi
Name:hbp
Encoded oniPlasmid IncFI ColV3-K300 Publication
OrganismiEscherichia coli
Taxonomic identifieri562 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Subcellular locationi

Hemoglobin-binding protease hbp translocator :

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane, Periplasm, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 52521 PublicationAdd
BLAST
Chaini53 – 13771325Hemoglobin-binding protease hbp autotransporterPRO_0000387597Add
BLAST
Chaini53 – 11001048Hemoglobin-binding protease hbpPRO_0000041982Add
BLAST
Chaini1101 – 1377277Hemoglobin-binding protease hbp translocatorPRO_0000041983Add
BLAST

Post-translational modificationi

Cleaved to release the mature protein from the outer membrane.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei1100 – 11012Cleavage

Keywords - PTMi

Zymogen

Proteomic databases

PRIDEiO88093.

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi54 – 596Combined sources
Helixi62 – 687Combined sources
Helixi72 – 743Combined sources
Beta strandi80 – 845Combined sources
Beta strandi90 – 945Combined sources
Turni107 – 1093Combined sources
Beta strandi113 – 1164Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi150 – 1534Combined sources
Beta strandi158 – 1614Combined sources
Helixi180 – 1823Combined sources
Turni184 – 1863Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi198 – 2014Combined sources
Beta strandi207 – 2115Combined sources
Beta strandi218 – 2225Combined sources
Beta strandi226 – 2283Combined sources
Turni229 – 2324Combined sources
Beta strandi233 – 2364Combined sources
Helixi244 – 2474Combined sources
Beta strandi249 – 2513Combined sources
Beta strandi262 – 2676Combined sources
Turni268 – 2714Combined sources
Beta strandi272 – 28413Combined sources
Beta strandi290 – 2945Combined sources
Helixi297 – 3059Combined sources
Helixi316 – 3183Combined sources
Beta strandi322 – 3265Combined sources
Turni328 – 3303Combined sources
Beta strandi332 – 3376Combined sources
Beta strandi340 – 3456Combined sources
Helixi352 – 3543Combined sources
Beta strandi357 – 3626Combined sources
Beta strandi365 – 3717Combined sources
Beta strandi379 – 3846Combined sources
Beta strandi386 – 3927Combined sources
Beta strandi396 – 4038Combined sources
Beta strandi408 – 4114Combined sources
Beta strandi420 – 43112Combined sources
Beta strandi434 – 4363Combined sources
Beta strandi439 – 4435Combined sources
Beta strandi445 – 4506Combined sources
Beta strandi466 – 4683Combined sources
Beta strandi474 – 4796Combined sources
Helixi485 – 4873Combined sources
Beta strandi488 – 4903Combined sources
Beta strandi495 – 4984Combined sources
Beta strandi504 – 5074Combined sources
Beta strandi516 – 5205Combined sources
Beta strandi522 – 5243Combined sources
Beta strandi526 – 5305Combined sources
Helixi536 – 5383Combined sources
Beta strandi555 – 5606Combined sources
Turni561 – 5644Combined sources
Beta strandi565 – 5717Combined sources
Beta strandi573 – 5753Combined sources
Beta strandi581 – 5833Combined sources
Beta strandi587 – 5915Combined sources
Helixi596 – 60712Combined sources
Beta strandi612 – 6143Combined sources
Beta strandi616 – 62712Combined sources
Beta strandi635 – 6384Combined sources
Beta strandi640 – 65718Combined sources
Helixi669 – 6779Combined sources
Beta strandi685 – 6873Combined sources
Beta strandi698 – 70912Combined sources
Beta strandi711 – 7144Combined sources
Beta strandi718 – 72811Combined sources
Beta strandi730 – 7345Combined sources
Beta strandi736 – 7416Combined sources
Turni742 – 7454Combined sources
Beta strandi746 – 7483Combined sources
Beta strandi752 – 7565Combined sources
Helixi762 – 7643Combined sources
Beta strandi767 – 77711Combined sources
Beta strandi779 – 7824Combined sources
Beta strandi784 – 79411Combined sources
Beta strandi796 – 7994Combined sources
Beta strandi802 – 8065Combined sources
Beta strandi808 – 8136Combined sources
Beta strandi815 – 8184Combined sources
Beta strandi823 – 8264Combined sources
Beta strandi830 – 84718Combined sources
Beta strandi854 – 8563Combined sources
Beta strandi859 – 87012Combined sources
Beta strandi874 – 8774Combined sources
Beta strandi879 – 89214Combined sources
Beta strandi894 – 8974Combined sources
Helixi909 – 9179Combined sources
Turni918 – 9203Combined sources
Beta strandi922 – 9276Combined sources
Beta strandi929 – 94517Combined sources
Beta strandi949 – 95810Combined sources
Beta strandi960 – 9634Combined sources
Beta strandi967 – 9693Combined sources
Beta strandi972 – 98211Combined sources
Beta strandi984 – 9885Combined sources
Beta strandi996 – 100611Combined sources
Beta strandi1008 – 10136Combined sources
Beta strandi1020 – 10223Combined sources
Beta strandi1026 – 10327Combined sources
Helixi1037 – 10393Combined sources
Beta strandi1040 – 10423Combined sources
Beta strandi1048 – 10514Combined sources
Beta strandi1053 – 10597Combined sources
Beta strandi1064 – 107310Combined sources
Helixi1075 – 109723Combined sources
Helixi1102 – 11065Combined sources
Beta strandi1115 – 112814Combined sources
Beta strandi1134 – 115017Combined sources
Beta strandi1153 – 117018Combined sources
Beta strandi1173 – 119018Combined sources
Beta strandi1193 – 121119Combined sources
Beta strandi1217 – 123418Combined sources
Beta strandi1236 – 125722Combined sources
Beta strandi1279 – 129214Combined sources
Beta strandi1294 – 131118Combined sources
Beta strandi1331 – 134515Combined sources
Turni1346 – 13483Combined sources
Beta strandi1349 – 136012Combined sources
Beta strandi1362 – 137716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXRX-ray2.20A53-1100[»]
3AEHX-ray2.00A/B1075-1377[»]
3AK5X-ray2.20A/B/C/D53-533[»]
A/B/C/D608-1100[»]
ProteinModelPortaliO88093.
SMRiO88093. Positions 1101-1377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO88093.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 302250Peptidase S6PROSITE-ProRule annotationAdd
BLAST
Domaini1111 – 1377267AutotransporterPROSITE-ProRule annotationAdd
BLAST

Domaini

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.

Sequence similaritiesi

Contains 1 autotransporter (TC 1.B.12) domain. [View classification]PROSITE-ProRule annotation
Contains 1 peptidase S6 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane beta strand

Family and domain databases

Gene3Di2.160.20.20. 3 hits.
2.40.128.130. 1 hit.
InterProiIPR005546. Autotransporte_beta.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR009003. Peptidase_S1_PA.
IPR000710. Peptidase_S6.
IPR030396. Peptidase_S6_dom.
[Graphical view]
PfamiPF03797. Autotransporter. 1 hit.
PF02395. Peptidase_S6. 1 hit.
[Graphical view]
PRINTSiPR00921. IGASERPTASE.
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF50494. SSF50494. 2 hits.
SSF51126. SSF51126. 3 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
PS51691. PEPTIDASE_S6. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O88093-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRIYSLRYS AVARGFIAVS EFARKCVHKS VRRLCFPVLL LIPVLFSAGS
60 70 80 90 100
LAGTVNNELG YQLFRDFAEN KGMFRPGATN IAIYNKQGEF VGTLDKAAMP
110 120 130 140 150
DFSAVDSEIG VATLINPQYI ASVKHNGGYT NVSFGDGENR YNIVDRNNAP
160 170 180 190 200
SLDFHAPRLD KLVTEVAPTA VTAQGAVAGA YLDKERYPVF YRLGSGTQYI
210 220 230 240 250
KDSNGQLTKM GGAYSWLTGG TVGSLSSYQN GEMISTSSGL VFDYKLNGAM
260 270 280 290 300
PIYGEAGDSG SPLFAFDTVQ NKWVLVGVLT AGNGAGGRGN NWAVIPLDFI
310 320 330 340 350
GQKFNEDNDA PVTFRTSEGG ALEWSFNSST GAGALTQGTT TYAMHGQQGN
360 370 380 390 400
DLNAGKNLIF QGQNGQINLK DSVSQGAGSL TFRDNYTVTT SNGSTWTGAG
410 420 430 440 450
IVVDNGVSVN WQVNGVKGDN LHKIGEGTLT VQGTGINEGG LKVGDGKVVL
460 470 480 490 500
NQQADNKGQV QAFSSVNIAS GRPTVVLTDE RQVNPDTVSW GYRGGTLDVN
510 520 530 540 550
GNSLTFHQLK AADYGAVLAN NVDKRATITL DYALRADKVA LNGWSESGKG
560 570 580 590 600
TAGNLYKYNN PYTNTTDYFI LKQSTYGYFP TDQSSNATWE FVGHSQGDAQ
610 620 630 640 650
KLVADRFNTA GYLFHGQLKG NLNVDNRLPE GVTGALVMDG AADISGTFTQ
660 670 680 690 700
ENGRLTLQGH PVIHAYNTQS VADKLAASGD HSVLTQPTSF SQEDWENRSF
710 720 730 740 750
TFDRLSLKNT DFGLGRNATL NTTIQADNSS VTLGDSRVFI DKNDGQGTAF
760 770 780 790 800
TLEEGTSVAT KDADKSVFNG TVNLDNQSVL NINDIFNGGI QANNSTVNIS
810 820 830 840 850
SDSAVLGNST LTSTALNLNK GANALASQSF VSDGPVNISD ATLSLNSRPD
860 870 880 890 900
EVSHTLLPVY DYAGSWNLKG DDARLNVGPY SMLSGNINVQ DKGTVTLGGE
910 920 930 940 950
GELSPDLTLQ NQMLYSLFNG YRNIWSGSLN APDATVSMTD TQWSMNGNST
960 970 980 990 1000
AGNMKLNRTI VGFNGGTSPF TTLTTDNLDA VQSAFVMRTD LNKADKLVIN
1010 1020 1030 1040 1050
KSATGHDNSI WVNFLKKPSN KDTLDIPLVS APEATADNLF RASTRVVGFS
1060 1070 1080 1090 1100
DVTPILSVRK EDGKKEWVLD GYQVARNDGQ GKAAATFMHI SYNNFITEVN
1110 1120 1130 1140 1150
NLNKRMGDLR DINGEAGTWV RLLNGSGSAD GGFTDHYTLL QMGADRKHEL
1160 1170 1180 1190 1200
GSMDLFTGVM ATYTDTDASA DLYSGKTKSW GGGFYASGLF RSGAYFDVIA
1210 1220 1230 1240 1250
KYIHNENKYD LNFAGAGKQN FRSHSLYAGA EVGYRYHLTD TTFVEPQAEL
1260 1270 1280 1290 1300
VWGRLQGQTF NWNDSGMDVS MRRNSVNPLV GRTGVVSGKT FSGKDWSLTA
1310 1320 1330 1340 1350
RAGLHYEFDL TDSADVHLKD AAGEHQINGR KDSRMLYGVG LNARFGDNTR
1360 1370
LGLEVERSAF GKYNTDDAIN ANIRYSF
Length:1,377
Mass (Da):148,257
Last modified:November 1, 1998 - v1
Checksum:iBB16D898EDAC0416
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223631 Genomic DNA. Translation: CAA11507.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ223631 Genomic DNA. Translation: CAA11507.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WXRX-ray2.20A53-1100[»]
3AEHX-ray2.00A/B1075-1377[»]
3AK5X-ray2.20A/B/C/D53-533[»]
A/B/C/D608-1100[»]
ProteinModelPortaliO88093.
SMRiO88093. Positions 1101-1377.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO88093.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO88093.

Family and domain databases

Gene3Di2.160.20.20. 3 hits.
2.40.128.130. 1 hit.
InterProiIPR005546. Autotransporte_beta.
IPR006315. OM_autotransptr_brl.
IPR012332. P22_tailspike_C-like.
IPR011050. Pectin_lyase_fold/virulence.
IPR009003. Peptidase_S1_PA.
IPR000710. Peptidase_S6.
IPR030396. Peptidase_S6_dom.
[Graphical view]
PfamiPF03797. Autotransporter. 1 hit.
PF02395. Peptidase_S6. 1 hit.
[Graphical view]
PRINTSiPR00921. IGASERPTASE.
SMARTiSM00869. Autotransporter. 1 hit.
[Graphical view]
SUPFAMiSSF103515. SSF103515. 1 hit.
SSF50494. SSF50494. 2 hits.
SSF51126. SSF51126. 3 hits.
TIGRFAMsiTIGR01414. autotrans_barl. 1 hit.
PROSITEiPS51208. AUTOTRANSPORTER. 1 hit.
PS51691. PEPTIDASE_S6. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 53-1100.
    Strain: O8:K43 / EB1.

Entry informationi

Entry nameiHBP_ECOLX
AccessioniPrimary (citable) accession number: O88093
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.