ID   HTPX_MYCMM              Reviewed;         286 AA.
AC   B2HRQ7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=MMAR_0912;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(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 membrane {ECO:0000255|HAMAP-Rule:MF_00188};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family. {ECO:0000255|HAMAP-
CC       Rule:MF_00188}.
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DR   EMBL; CP000854; ACC39369.1; -; Genomic_DNA.
DR   RefSeq; WP_012392834.1; NC_010612.1.
DR   AlphaFoldDB; B2HRQ7; -.
DR   STRING; 216594.MMAR_0912; -.
DR   EnsemblBacteria; ACC39369; ACC39369; MMAR_0912.
DR   GeneID; 64259649; -.
DR   KEGG; mmi:MMAR_0912; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_042266_3_1_11; -.
DR   OMA; AVCCTEG; -.
DR   OrthoDB; 1918093at2; -.
DR   Proteomes; UP000001190; 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.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW   Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT   CHAIN           1..286
FT                   /note="Protease HtpX homolog"
FT                   /id="PRO_1000098827"
FT   TRANSMEM        13..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        34..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   ACT_SITE        136
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         139
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   286 AA;  30880 MW;  A3B531D4FB315438 CRC64;
     MTWHPHANRL KTFLLLVGMS AMIVFFGALF GRTALILAVL FAVGMNVYVY FNSDKLALRA
     MHAQPVSELQ APAMYRIVRE LATSAHQPMP RLYISDTAAP NAFATGRNPR NAAVCCTTGI
     LALLNERELR AVLGHELSHV YNRDILISCI AGALASVITA LANMAMWAGM FGGNRDGQNP
     FALLLVSLLG PIAATVVRMA VSRSREYQAD ESGAVLTGDP LALASALRKI SGGVQLAPLP
     PEPQLASQAH LMIANPFRAG ERIGSLFSTH PPIEDRIRRL EQMARG