ID W9DN16_METTI Unreviewed; 293 AA.
AC W9DN16;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=MettiDRAFT_0734 {ECO:0000313|EMBL:ETA67319.1};
OS Methanolobus tindarius DSM 2278.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanolobus.
OX NCBI_TaxID=1090322 {ECO:0000313|EMBL:ETA67319.1, ECO:0000313|Proteomes:UP000019483};
RN [1] {ECO:0000313|EMBL:ETA67319.1, ECO:0000313|Proteomes:UP000019483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2278 {ECO:0000313|EMBL:ETA67319.1,
RC ECO:0000313|Proteomes:UP000019483};
RG DOE Joint Genome Institute;
RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (AUG-2013) 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:ETA67319.1}.
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DR EMBL; AZAJ01000001; ETA67319.1; -; Genomic_DNA.
DR RefSeq; WP_023844455.1; NZ_AZAJ01000001.1.
DR AlphaFoldDB; W9DN16; -.
DR STRING; 1090322.MettiDRAFT_0734; -.
DR MEROPS; M48.004; -.
DR OrthoDB; 28389at2157; -.
DR Proteomes; UP000019483; 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; cd07327; 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 Stress response {ECO:0000313|EMBL:ETA67319.1};
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..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 148..165
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 185..206
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT DOMAIN 72..287
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
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 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ SEQUENCE 293 AA; 32428 MW; 6685509BA4C1A781 CRC64;
MVEWKKDLGL EGRMLLTMFL LAAVYLGFLV FISQYTSASF MLLFVMLFMG AQYYYSDKLV
LWSTGAHVVS EAEEPKLHET ITRLCVIAGL PKPTVAVVNT SVPNAFATGR SPKKAVVAVT
TGLMHKLDQG ELEAVLAHEL SHVKNRDMAV LTIASFISTL AFYIVRYSFY FGGFGGNRRN
SNGGLIAIWI VSIIVWVLSF LLIRALSRYR EFAADRGSAL ITGQPTQLIS ALRKISGTMA
NVPTEDLRKV EGMNAFFIIP AAVSGSVMNM LSTHPSMEKR IAALEKIQRE IEY
//
