ID A0A162FLP8_9EURY Unreviewed; 318 AA.
AC A0A162FLP8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=MBORA_13900 {ECO:0000313|EMBL:KZX11850.1};
OS Methanobrevibacter oralis.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=66851 {ECO:0000313|EMBL:KZX11850.1, ECO:0000313|Proteomes:UP000077428};
RN [1] {ECO:0000313|EMBL:KZX11850.1, ECO:0000313|Proteomes:UP000077428}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7256 {ECO:0000313|EMBL:KZX11850.1,
RC ECO:0000313|Proteomes:UP000077428};
RA Poehlein A., Seedorf H., Daniel R.;
RT "Genome sequence of Methanobrevibacter oralis DSM 7256.";
RL Submitted (APR-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}.
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:KZX11850.1}.
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DR EMBL; LWMU01000081; KZX11850.1; -; Genomic_DNA.
DR RefSeq; WP_063720437.1; NZ_LWMU01000081.1.
DR AlphaFoldDB; A0A162FLP8; -.
DR STRING; 66851.MBORA_13900; -.
DR PATRIC; fig|66851.6.peg.1508; -.
DR OrthoDB; 28389at2157; -.
DR Proteomes; UP000077428; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; cd07338; 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; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
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; PF13202; EF-hand_5; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR PROSITE; PS00018; EF_HAND_1; 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 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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 39..60
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 148..171
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 177..199
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT DOMAIN 71..316
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT DOMAIN 261..283
FT /note="EF-hand"
FT /evidence="ECO:0000259|Pfam:PF13202"
FT ACT_SITE 139
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ SEQUENCE 318 AA; 35820 MW; 543F0FCFB4429686 CRC64;
MRGTWKLKLR MWLTTILMFT IVYFLVSLAG AYLGISGGYF FLIVSLIIVF LQYWFGPSIV
KRSMNVRPLS PQEAPHIHQM VEELSQAAGI PKPEIGLSEI NIPNAFAYGR TSRSGHIAIT
HPILGLLDRD ELKAVLGHEM GHLKHNDMAI TAMVSVIPMI CYYIALSFMF SRNNNNGGFI
IGIVGYVFYL IGQLLVLFIS RIREYYADEA SVEFGNRPAA LVSALYKLSY GAAKVDSQII
NEVNTTRAFF INDVNNAQSD INEFRQIDYN GDGSISDDEL RRLNNARIEV STSKKLMEIL
STHPDTLKRV KRLSELEN
//
