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Database: UniProt
Entry: A0A1X9N551_9GAMM
LinkDB: A0A1X9N551_9GAMM
Original site: A0A1X9N551_9GAMM 
ID   A0A1X9N551_9GAMM        Unreviewed;       295 AA.
AC   A0A1X9N551;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Protease HtpX {ECO:0000256|HAMAP-Rule:MF_00188};
DE            EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_00188};
DE   AltName: Full=Heat shock protein HtpX {ECO:0000256|HAMAP-Rule:MF_00188};
GN   Name=htpX {ECO:0000256|HAMAP-Rule:MF_00188};
GN   ORFNames=BST96_03475 {ECO:0000313|EMBL:ARN73248.1};
OS   Oceanicoccus sagamiensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; Oceanicoccus.
OX   NCBI_TaxID=716816 {ECO:0000313|EMBL:ARN73248.1, ECO:0000313|Proteomes:UP000193450};
RN   [1] {ECO:0000313|EMBL:ARN73248.1, ECO:0000313|Proteomes:UP000193450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 107125 {ECO:0000313|EMBL:ARN73248.1,
RC   ECO:0000313|Proteomes:UP000193450};
RA   Kumagai Y.;
RT   "Trade-off between light-utilization and light-protection in marine
RT   flavobacteria.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00188};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00188};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00188};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00188}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family.
CC       {ECO:0000256|ARBA:ARBA00009779, ECO:0000256|HAMAP-Rule:MF_00188}.
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DR   EMBL; CP019343; ARN73248.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X9N551; -.
DR   STRING; 716816.BST96_03475; -.
DR   KEGG; osg:BST96_03475; -.
DR   OrthoDB; 15218at2; -.
DR   Proteomes; UP000193450; Chromosome.
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   CDD; cd07335; M48B_HtpX_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
DR   InterPro; IPR022919; Pept_M48_protease_HtpX.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR   PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00188};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00188};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00188};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193450};
KW   Stress response {ECO:0000256|HAMAP-Rule:MF_00188};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00188}.
FT   TRANSMEM        42..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        157..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        195..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   DOMAIN          81..293
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   ACT_SITE        148
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         151
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         224
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   295 AA;  31657 MW;  83CFF6F03086CF2E CRC64;
     MLRIFLFLAT NMAILLVASI TLSLLGFNSI MAANGVDLNL TALLVFCAVF GMGGSLVSLM
     LSKWMAKRSM GVVLIDQPKN RQEQWLKDTV AELAQKAGIG MPEVGIFPSP SSNAFATGAS
     RNNALVAVSA GLLERFSPEE AKAVMAHEIG HVANGDMITL SLIQGVVNTF VMFFARIIGH
     AFDRIVLKNE RGFGIGAWIA TIVAEMILGF LASTIVFWFS RRREFRADVA GAELASRSGM
     IAALQRLRAE QGLPNDMPGE MAAFGISGPM KEGLMSLFLT HPPLEKRIAA LQAGA
//
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