HAPT_VIBCH
ID HAPT_VIBCH Reviewed; 609 AA.
AC P24153; Q9JPZ3;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Hemagglutinin/proteinase;
DE Short=HA/protease;
DE EC=3.4.24.-;
DE AltName: Full=Vibriolysin;
DE Flags: Precursor;
GN Name=hap; OrderedLocusNames=VC_A0865;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3083;
RX PubMed=2045361; DOI=10.1128/jb.173.11.3311-3317.1991;
RA Haese C.C., Finkelstein R.A.;
RT "Cloning and nucleotide sequence of the Vibrio cholerae
RT hemagglutinin/protease (HA/protease) gene and construction of an
RT HA/protease-negative strain.";
RL J. Bacteriol. 173:3311-3317(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
RN [3]
RP PROTEIN SEQUENCE OF 197-217.
RC STRAIN=Classical CA401;
RX PubMed=2123831; DOI=10.1128/iai.58.12.4011-4015.1990;
RA Haese C.C., Finkelstein R.A.;
RT "Comparison of the Vibrio cholerae hemagglutinin/protease and the
RT Pseudomonas aeruginosa elastase.";
RL Infect. Immun. 58:4011-4015(1990).
CC -!- FUNCTION: May play a role in the pathogenesis of cholera. Hap nicks and
CC activates the A subunit of cholera enterotoxin and related
CC enterotoxins.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
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DR EMBL; M59466; AAA27579.1; -; Genomic_DNA.
DR EMBL; AE003853; AAF96763.1; -; Genomic_DNA.
DR PIR; A42358; A42358.
DR RefSeq; NP_233251.1; NC_002506.1.
DR RefSeq; WP_000782181.1; NZ_LT906615.1.
DR AlphaFoldDB; P24153; -.
DR SMR; P24153; -.
DR STRING; 243277.VC_A0865; -.
DR MEROPS; M04.003; -.
DR DNASU; 2612874; -.
DR EnsemblBacteria; AAF96763; AAF96763; VC_A0865.
DR KEGG; vch:VC_A0865; -.
DR PATRIC; fig|243277.26.peg.3481; -.
DR eggNOG; COG3227; Bacteria.
DR HOGENOM; CLU_008590_4_2_6; -.
DR OMA; QLYWTAN; -.
DR BioCyc; VCHO:VCA0865-MON; -.
DR BRENDA; 3.4.24.25; 6626.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.390.10; -; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW Metalloprotease; Protease; Reference proteome; Secreted; Signal; Zinc;
KW Zymogen.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..196
FT /evidence="ECO:0000255"
FT /id="PRO_0000028628"
FT CHAIN 197..609
FT /note="Hemagglutinin/proteinase"
FT /id="PRO_0000028629"
FT ACT_SITE 344
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT ACT_SITE 426
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 343
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 609 AA; 65891 MW; 6D003A589B956FD0 CRC64;
MKMIQRPLNW LVLAGAATGF PLYAAQMVTI DDASMVEQAL AQQQYSMMPA ASGFKAVNTV
QLPNGKVKVR YQQMYNGVPV YGTVVVATES SKGISQVYGQ MAQQLEADLP TVTPDIESQQ
AIALAVSHFG EQHAGESLPV ENESVQLMVR LDDNQQAQLV YLVDFFVASE TPSRPFYFIS
AETGEVLDQW DGINHAQATG TGPGGNQKTG RYEYGSNGLP GFTIDKTGTT CTMNNSAVKT
VNLNGGTSGS TAFSYACNNS TNYNSVKTVN GAYSPLNDAH FFGKVVFDMY QQWLNTSPLT
FQLTMRVHYG NNYENAFWDG RAMTFGDGYT RFYPLVDINV SAHEVSHGFT EQNSGLVYRD
MSGGINEAFS DIAGEAAEYF MRGNVDWIVG ADIFKSSGGL RYFDQPSRDG RSIDHASQYY
SGIDVHHSSG VFNRAFYLLA NKSGWNVRKG FEVFAVANQL YWTPNSTFDQ GGCGVVKAAQ
DLNYNTADVV AAFNTVGVNA SCGTTPPPVG KVLEKGKPIT GLSGSRGGED FYTFTVTNSG
SVVVSISGGT GDADLYVKAG SKPTTSSWDC RPYRSGNAEQ CSISAVVGTT YHVMLRGYSN
YSGVTLRLD
