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HTPX_PYRAB
ID   HTPX_PYRAB              Reviewed;         289 AA.
AC   Q9UZK3; G8ZKB6;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
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=PYRAB11430;
GN   ORFNames=PAB0758;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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}.
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DR   EMBL; AJ248286; CAB50054.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE70559.1; -; Genomic_DNA.
DR   PIR; A75094; A75094.
DR   RefSeq; WP_010868260.1; NC_000868.1.
DR   AlphaFoldDB; Q9UZK3; -.
DR   SMR; Q9UZK3; -.
DR   STRING; 272844.PAB0758; -.
DR   EnsemblBacteria; CAB50054; CAB50054; PAB0758.
DR   GeneID; 1496505; -.
DR   KEGG; pab:PAB0758; -.
DR   PATRIC; fig|272844.11.peg.1200; -.
DR   eggNOG; arCOG01331; Archaea.
DR   HOGENOM; CLU_042266_3_0_2; -.
DR   OMA; SRYREYV; -.
DR   OrthoDB; 62484at2157; -.
DR   PhylomeDB; Q9UZK3; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
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   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..289
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_0000138923"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   289 AA;  31696 MW;  B0D16B0976DAEE0D CRC64;
     MGLGLWIRTG VLMAFLTALL VGIGYLIGGR GGMIIAFTIA LFMNLISYWF SDSIVLSWYN
     ARIVSEEEAP ELHYIVEKLA RQAGIPKPKV AIVPTMVPNA FATGRGPGNA VVAVTEGLLH
     LLNRDELEGV IAHEISHIKN RDTLIQTLAA VLAGAIMILV DFARWSLWFG AYDDERDSGS
     VIGLILAIVL APLAATLIQL AISRSREYLA DETGARISGK PHALASALMK IEEAIRYRPL
     RRGNPATAHM FIVNPFRGVD FAELFSTHPP TEKRIERLRK IALEMGIVF
 
 
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