(data stored in ACNUC30630 zone)

SWISSPROT: HTPX_TROW8

ID   HTPX_TROW8              Reviewed;         291 AA.
AC   Q83IG0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   11-DEC-2019, entry version 99.
DE   RecName: Full=Protease HtpX homolog {ECO:0000255|HAMAP-Rule:MF_00188};
DE            EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188};
GN   Name=htpX {ECO:0000255|HAMAP-Rule:MF_00188}; OrderedLocusNames=TW013;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00188};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00188};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00188};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00188}.
DR   EMBL; BX251410; CAD66705.1; -; Genomic_DNA.
DR   PRIDE; Q83IG0; -.
DR   EnsemblBacteria; CAD66705; CAD66705; TW013.
DR   KEGG; tws:TW013; -.
DR   HOGENOM; HOG000227301; -.
DR   KO; K03799; -.
DR   OMA; AVCCTEG; -.
DR   BioCyc; GCF_000196075:G1EE9-15-MONOMER; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
DR   InterPro; IPR022919; Pept_M48_protease_HtpX.
DR   InterPro; IPR001915; Peptidase_M48.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q83IG0.
DR   SWISS-2DPAGE; Q83IG0.
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..291
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_1000020963"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        155..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   METAL           140
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   METAL           144
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   METAL           215
FT                   /note="Zinc; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   291 AA;  32179 MW;  AFB073197CBFE08E CRC64;
     MMYSFIARNK INTFLILFVF ILACGGFGLL AGRFLGMSFF LFILLLAAGY ACVQYFFSGR
     LAVLMSGARK ISRNDNPRLW NTVENLSITT GLPMPEVYIV DDPAPNAFAT GRDPKHAKVA
     ATSGLLEILD DSELEGVMAH EMGHVKNYDI RVSTIVFGLV SAVGLISDMV LRALIWGDNR
     REGNSAFSFA IVLFFSLLAP IAAMLVQLAV SREREYLADA TGALTTRYPA ALASALAKLE
     GNARPLQRQS SSMAHLWISN PMPRGFFRKL FSTHPPTEER IRRLKEMGNQ F
//

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