ID W3RKM7_9BRAD Unreviewed; 388 AA.
AC W3RKM7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Protease HtpX homolog {ECO:0000256|HAMAP-Rule:MF_00188};
DE EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_00188};
GN Name=htpX {ECO:0000256|HAMAP-Rule:MF_00188};
GN ORFNames=X566_03735 {ECO:0000313|EMBL:ETR76834.1};
OS Afipia sp. P52-10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1429916 {ECO:0000313|EMBL:ETR76834.1, ECO:0000313|Proteomes:UP000018975};
RN [1] {ECO:0000313|Proteomes:UP000018975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P52-10 {ECO:0000313|Proteomes:UP000018975};
RX PubMed=25874801;
RA Pickering B.S., Tyler S., Smith G., Burton L., Li M., Dallaire A.,
RA Weingartl H.;
RT "Identification of a novel afipia species isolated from an Indian flying
RT fox.";
RL PLoS ONE 10:E0121274-E0121274(2015).
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}.
CC -!- SIMILARITY: Belongs to the peptidase M48B family.
CC {ECO:0000256|ARBA:ARBA00009779, ECO:0000256|HAMAP-Rule:MF_00188}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ETR76834.1}.
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DR EMBL; AZSJ01000003; ETR76834.1; -; Genomic_DNA.
DR RefSeq; WP_034463537.1; NZ_AZSJ01000003.1.
DR AlphaFoldDB; W3RKM7; -.
DR STRING; 1429916.X566_03735; -.
DR PATRIC; fig|1429916.3.peg.755; -.
DR eggNOG; COG0501; Bacteria.
DR OrthoDB; 15218at2; -.
DR Proteomes; UP000018975; Unassembled WGS sequence.
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; cd07340; 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:SF2; PROTEASE HTPX HOMOLOG; 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:UP000018975};
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 18..43
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 176..199
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 228..249
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT DOMAIN 98..326
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REGION 344..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 165
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ SEQUENCE 388 AA; 41418 MW; DA5D375D5A7CEFC6 CRC64;
MAAYGLYTHI ASNKTRSILL LVGLFLLIYV MVYAGALIAE VFLSPDRTVD YYLRAAWVDL
YKALPIATIV SAIWIVIAYF FNQAIIDAVT GGHTVTRKEQ PRLYNLLENL CISRGIPMPR
LKIMETDALN AFASGLNPRQ YSITVTSGLL KNLDDQEVEA VLGHELTHIR NGDVQLMVVA
VIIAGVVGFF AELVFRMVFN SRWSFGGGSG GRSSSSSDGD RKGGGGGAIV AILIAVVLIA
LAWFLSLVVR FALSRSREFL ADAGSVELTK NPDAMISALR KIENRGELEG VTSSVMEMCV
DNPREGFADL FATHPSVDSR VRALVKFAGG HDPGRLADLQ NAQITPAGGS VPDAGGAMPT
DASPASHPGP WGSPAAPASP FGGPTLRQ
//
