HTPX_METI4
ID HTPX_METI4 Reviewed; 300 AA.
AC B3DX74;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Minf_1729;
OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS V4)).
OC Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum.
OX NCBI_TaxID=481448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate V4;
RX PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA Feng L., Wang L., Alam M.;
RT "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT Verrucomicrobia.";
RL Biol. Direct 3:26-26(2008).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00188}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00188}.
CC -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000255|HAMAP-
CC Rule:MF_00188}.
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DR EMBL; CP000975; ACD83783.1; -; Genomic_DNA.
DR RefSeq; WP_012464065.1; NC_010794.1.
DR AlphaFoldDB; B3DX74; -.
DR SMR; B3DX74; -.
DR MEROPS; M48.002; -.
DR EnsemblBacteria; ACD83783; ACD83783; Minf_1729.
DR KEGG; min:Minf_1729; -.
DR eggNOG; COG0501; Bacteria.
DR HOGENOM; CLU_042266_1_0_0; -.
DR OMA; AVCCTEG; -.
DR OrthoDB; 1918093at2; -.
DR Proteomes; UP000009149; 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 inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..300
FT /note="Protease HtpX homolog"
FT /id="PRO_1000192745"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT ACT_SITE 147
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 146
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ SEQUENCE 300 AA; 33426 MW; D2760C1144618C7F CRC64;
MFKRIFLLTL TNIAVIFLLT LFISLLHLDR WLNAYGIDYQ TLFLFSMVVG FTGSFISLAI
SKWMAKMAYN IHVIQEPSNE AERWLVETVA ELAKRANIRM PEVGIYESPE VNAFATGPSR
SNALVAVSTG ILSQMNKKQI AGVLAHEITH INNGDMVTMT LLQGVVNTFV VFLSRIIGFF
VDRLFSRNEE RESIGIGFYL GMFISEIVLG LLASIIVAWY SRMREFRADA GGAHLAGKEA
MISALKKLKQ IMEGESAFID ERSPALNAFK INGRPGGILA LLATHPPLDE RIKALERIPD