HBP_ECOLX
ID HBP_ECOLX Reviewed; 1377 AA.
AC O88093;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Hemoglobin-binding protease hbp autotransporter;
DE EC=3.4.21.-;
DE Contains:
DE RecName: Full=Hemoglobin-binding protease hbp;
DE Contains:
DE RecName: Full=Hemoglobin-binding protease hbp translocator;
DE AltName: Full=Helper peptide;
DE Flags: Precursor;
GN Name=hbp;
OS Escherichia coli.
OG Plasmid IncFI ColV3-K30.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 53-66, FUNCTION,
RP SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=O8:K43 / EB1;
RX PubMed=9743528; DOI=10.1084/jem.188.6.1091;
RA Otto B.R., van Dooren S.J.M., Nuijens J.H., Luirink J., Oudega B.;
RT "Characterization of a hemoglobin protease secreted by the pathogenic
RT Escherichia coli strain EB1.";
RL J. Exp. Med. 188:1091-1103(1998).
RN [2]
RP FUNCTION.
RC STRAIN=O8:K43 / EB1;
RX PubMed=11748157; DOI=10.1128/iai.70.1.5-10.2002;
RA Otto B.R., van Dooren S.J.M., Dozois C.M., Luirink J., Oudega B.;
RT "Escherichia coli hemoglobin protease autotransporter contributes to
RT synergistic abscess formation and heme-dependent growth of Bacteroides
RT fragilis.";
RL Infect. Immun. 70:5-10(2002).
RN [3]
RP SECRETION.
RC STRAIN=O8:K43 / EB1;
RX PubMed=12466262; DOI=10.1074/jbc.m211630200;
RA Sijbrandi R., Urbanus M.L., ten Hagen-Jongman C.M., Bernstein H.D.,
RA Oudega B., Otto B.R., Luirink J.;
RT "Signal recognition particle (SRP)-mediated targeting and Sec-dependent
RT translocation of an extracellular Escherichia coli protein.";
RL J. Biol. Chem. 278:4654-4659(2003).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 53-1100.
RC STRAIN=O8:K43 / EB1;
RX PubMed=15728184; DOI=10.1074/jbc.m412885200;
RA Otto B.R., Sijbrandi R., Luirink J., Oudega B., Heddle J.G., Mizutani K.,
RA Park S.-Y., Tame J.R.H.;
RT "Crystal structure of hemoglobin protease, a heme binding autotransporter
RT protein from pathogenic Escherichia coli.";
RL J. Biol. Chem. 280:17339-17345(2005).
CC -!- FUNCTION: Interacts with hemoglobin, degrades it and subsequently binds
CC the released heme. Could make heme accessible not only for E.coli, but
CC also for B.fragilis during mixed intra-abdominal infections. Has a role
CC in abscess formation. {ECO:0000269|PubMed:11748157,
CC ECO:0000269|PubMed:9743528}.
CC -!- ACTIVITY REGULATION: Protease activity is inhibited by 3,4-
CC dichloroisocoumarin.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:9743528};
CC -!- SUBCELLULAR LOCATION: [Hemoglobin-binding protease hbp
CC autotransporter]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Hemoglobin-binding protease hbp]: Secreted. Cell
CC surface.
CC -!- SUBCELLULAR LOCATION: [Hemoglobin-binding protease hbp translocator]:
CC Cell outer membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter
CC domain) is localized in the outer membrane. {ECO:0000250}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface, with subsequent cleavage.
CC -!- PTM: Cleaved to release the mature protein from the outer membrane.
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DR EMBL; AJ223631; CAA11507.1; -; Genomic_DNA.
DR RefSeq; WP_021534952.1; NZ_UGFJ01000001.1.
DR PDB; 1WXR; X-ray; 2.20 A; A=53-1100.
DR PDB; 3AEH; X-ray; 2.00 A; A/B=1075-1377.
DR PDB; 3AK5; X-ray; 2.20 A; A/B/C/D=53-533, A/B/C/D=608-1100.
DR PDBsum; 1WXR; -.
DR PDBsum; 3AEH; -.
DR PDBsum; 3AK5; -.
DR AlphaFoldDB; O88093; -.
DR SMR; O88093; -.
DR MEROPS; S06.003; -.
DR EvolutionaryTrace; O88093; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02395; Peptidase_S6; 1.
DR PRINTS; PR00921; IGASERPTASE.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF51126; SSF51126; 2.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Hydrolase;
KW Membrane; Periplasm; Plasmid; Protease; Secreted; Serine protease; Signal;
KW Transmembrane; Transmembrane beta strand; Virulence; Zymogen.
FT SIGNAL 1..52
FT /evidence="ECO:0000269|PubMed:9743528"
FT CHAIN 53..1377
FT /note="Hemoglobin-binding protease hbp autotransporter"
FT /id="PRO_0000387597"
FT CHAIN 53..1100
FT /note="Hemoglobin-binding protease hbp"
FT /id="PRO_0000041982"
FT CHAIN 1101..1377
FT /note="Hemoglobin-binding protease hbp translocator"
FT /id="PRO_0000041983"
FT DOMAIN 53..302
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1111..1377
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT ACT_SITE 125
FT /note="Charge relay system"
FT ACT_SITE 153
FT /note="Charge relay system"
FT ACT_SITE 259
FT /note="Charge relay system"
FT SITE 1100..1101
FT /note="Cleavage"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 62..68
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 80..84
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1WXR"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1WXR"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:1WXR"
FT TURN 229..232
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:1WXR"
FT TURN 268..271
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 272..284
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 290..294
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 297..305
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:1WXR"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 332..337
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 352..354
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 357..362
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 379..384
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 396..403
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 420..431
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 445..450
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 474..479
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 495..498
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 516..520
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 522..524
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 526..530
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 555..560
FT /evidence="ECO:0007829|PDB:1WXR"
FT TURN 561..564
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 573..575
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 581..583
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 596..607
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 616..627
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 635..638
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 640..657
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 669..677
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 698..709
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 711..714
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 718..728
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 730..734
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 736..741
FT /evidence="ECO:0007829|PDB:1WXR"
FT TURN 742..745
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 746..748
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 752..756
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 762..764
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 767..777
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 779..782
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 784..794
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 796..799
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 802..806
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 808..813
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 815..818
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 823..826
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 830..847
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 854..856
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 859..870
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 874..877
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 879..892
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 894..897
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 909..917
FT /evidence="ECO:0007829|PDB:1WXR"
FT TURN 918..920
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 922..927
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 929..945
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 949..958
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 960..963
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:3AK5"
FT STRAND 972..982
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 984..988
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 996..1006
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 1008..1013
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 1020..1022
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 1026..1032
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 1037..1039
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 1040..1042
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 1048..1051
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 1053..1059
FT /evidence="ECO:0007829|PDB:1WXR"
FT STRAND 1064..1073
FT /evidence="ECO:0007829|PDB:1WXR"
FT HELIX 1075..1097
FT /evidence="ECO:0007829|PDB:3AEH"
FT HELIX 1102..1106
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1115..1128
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1134..1150
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1153..1170
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1173..1190
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1193..1211
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1217..1234
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1236..1257
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1279..1292
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1294..1311
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1331..1345
FT /evidence="ECO:0007829|PDB:3AEH"
FT TURN 1346..1348
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1349..1360
FT /evidence="ECO:0007829|PDB:3AEH"
FT STRAND 1362..1377
FT /evidence="ECO:0007829|PDB:3AEH"
SQ SEQUENCE 1377 AA; 148257 MW; BB16D898EDAC0416 CRC64;
MNRIYSLRYS AVARGFIAVS EFARKCVHKS VRRLCFPVLL LIPVLFSAGS LAGTVNNELG
YQLFRDFAEN KGMFRPGATN IAIYNKQGEF VGTLDKAAMP DFSAVDSEIG VATLINPQYI
ASVKHNGGYT NVSFGDGENR YNIVDRNNAP SLDFHAPRLD KLVTEVAPTA VTAQGAVAGA
YLDKERYPVF YRLGSGTQYI KDSNGQLTKM GGAYSWLTGG TVGSLSSYQN GEMISTSSGL
VFDYKLNGAM PIYGEAGDSG SPLFAFDTVQ NKWVLVGVLT AGNGAGGRGN NWAVIPLDFI
GQKFNEDNDA PVTFRTSEGG ALEWSFNSST GAGALTQGTT TYAMHGQQGN DLNAGKNLIF
QGQNGQINLK DSVSQGAGSL TFRDNYTVTT SNGSTWTGAG IVVDNGVSVN WQVNGVKGDN
LHKIGEGTLT VQGTGINEGG LKVGDGKVVL NQQADNKGQV QAFSSVNIAS GRPTVVLTDE
RQVNPDTVSW GYRGGTLDVN GNSLTFHQLK AADYGAVLAN NVDKRATITL DYALRADKVA
LNGWSESGKG TAGNLYKYNN PYTNTTDYFI LKQSTYGYFP TDQSSNATWE FVGHSQGDAQ
KLVADRFNTA GYLFHGQLKG NLNVDNRLPE GVTGALVMDG AADISGTFTQ ENGRLTLQGH
PVIHAYNTQS VADKLAASGD HSVLTQPTSF SQEDWENRSF TFDRLSLKNT DFGLGRNATL
NTTIQADNSS VTLGDSRVFI DKNDGQGTAF TLEEGTSVAT KDADKSVFNG TVNLDNQSVL
NINDIFNGGI QANNSTVNIS SDSAVLGNST LTSTALNLNK GANALASQSF VSDGPVNISD
ATLSLNSRPD EVSHTLLPVY DYAGSWNLKG DDARLNVGPY SMLSGNINVQ DKGTVTLGGE
GELSPDLTLQ NQMLYSLFNG YRNIWSGSLN APDATVSMTD TQWSMNGNST AGNMKLNRTI
VGFNGGTSPF TTLTTDNLDA VQSAFVMRTD LNKADKLVIN KSATGHDNSI WVNFLKKPSN
KDTLDIPLVS APEATADNLF RASTRVVGFS DVTPILSVRK EDGKKEWVLD GYQVARNDGQ
GKAAATFMHI SYNNFITEVN NLNKRMGDLR DINGEAGTWV RLLNGSGSAD GGFTDHYTLL
QMGADRKHEL GSMDLFTGVM ATYTDTDASA DLYSGKTKSW GGGFYASGLF RSGAYFDVIA
KYIHNENKYD LNFAGAGKQN FRSHSLYAGA EVGYRYHLTD TTFVEPQAEL VWGRLQGQTF
NWNDSGMDVS MRRNSVNPLV GRTGVVSGKT FSGKDWSLTA RAGLHYEFDL TDSADVHLKD
AAGEHQINGR KDSRMLYGVG LNARFGDNTR LGLEVERSAF GKYNTDDAIN ANIRYSF
