ID   HIP1_MYCBO              Reviewed;         520 AA.
AC   P65824; A0A1R3Y0R1; Q10509; X2BJM9;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Serine protease Hip1 {ECO:0000250|UniProtKB:P9WHR3};
DE            EC=3.4.21.- {ECO:0000250|UniProtKB:P9WHR3};
DE   Flags: Precursor;
GN   Name=hip1 {ECO:0000250|UniProtKB:P9WHR3}; OrderedLocusNames=BQ2027_MB2248C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
CC   -!- FUNCTION: Serine protease that promotes pathogenesis by promoting the
CC       processing and the extracellular release of the M.bovis heat-shock
CC       protein GroEL2. {ECO:0000250|UniProtKB:P9WHR3}.
CC   -!- FUNCTION: Key immunomodulatory virulence factor, which promotes
CC       survival in host macrophages and modulates host immune responses.
CC       {ECO:0000250|UniProtKB:P9WHR3}.
CC   -!- SUBCELLULAR LOCATION: Cell envelope {ECO:0000250|UniProtKB:P9WHR3}.
CC       Cell membrane {ECO:0000255|PROSITE-ProRule:PRU00303}; Lipid-anchor
CC       {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; LT708304; SIU00856.1; -; Genomic_DNA.
DR   RefSeq; NP_855897.1; NC_002945.3.
DR   RefSeq; WP_003411486.1; NC_002945.4.
DR   AlphaFoldDB; P65824; -.
DR   SMR; P65824; -.
DR   ESTHER; myctu-ym24; AlphaBeta_hydrolase.
DR   MEROPS; S33.023; -.
DR   EnsemblBacteria; SIU00856; SIU00856; BQ2027_MB2248C.
DR   GeneID; 45426201; -.
DR   PATRIC; fig|233413.5.peg.2465; -.
DR   OMA; LNCAYWP; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0031975; C:envelope; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           31..520
FT                   /note="Serine protease Hip1"
FT                   /id="PRO_0000027330"
FT   DOMAIN          102..497
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        228
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHR3"
FT   ACT_SITE        463
FT                   /evidence="ECO:0000250|UniProtKB:P9WHR3"
FT   ACT_SITE        490
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P9WHR3"
FT   LIPID           31
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           31
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   520 AA;  55924 MW;  8DC560534ABE9B0E CRC64;
     MGMRLSRRDK IARMLLIWAA LAAVALVLVG CIRVVGGRAR MAEPKLGQPV EWTPCRSSNP
     QVKIPGGALC GKLAVPVDYD RPDGDVAALA LIRFPATGDK IGSLVINPGG PGESGIEAAL
     GVFQTLPKRV HERFDLVGFD PRGVASSRPA IWCNSDADND RLRAEPQVDY SREGVAHIEN
     ETKQFVGRCV DKMGKNFLAH VGTVNVAKDL DAIRAALGDD KLTYLGYSYG TRIGSAYAEE
     FPQRVRAMIL DGAVDPNADP IEAELRQAKG FQDAFNNYAA DCAKNAGCPL GADPAKAVEV
     YHSLVDPLVD PDNPRISRPA RTKDPRGLSY SDAIVGTIMA LYSPNLWQHL TDGLSELVDN
     RGDTLLALAD MYMRRDSHGR YNNSGDARVA INCVDQPPVT DRDKVIDEDR RAREIAPFMS
     YGKFTGDAPL GTCAFWPVPP TSQPHAVSAP GLVPTVVVST THDPATPYKA GVDLANQLRG
     SLLTFDGTQH TVVFQGDSCI DEYVTAYLIG GTTPPSGAKC