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Database: UniProt
Entry: A0A2T5X6B0_9MICO
LinkDB: A0A2T5X6B0_9MICO
Original site: A0A2T5X6B0_9MICO 
ID   A0A2T5X6B0_9MICO        Unreviewed;       297 AA.
AC   A0A2T5X6B0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=C8A06_0320 {ECO:0000313|EMBL:PTW90629.1};
OS   Microbacteriaceae bacterium MWH-Ta3.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae.
OX   NCBI_TaxID=207608 {ECO:0000313|EMBL:PTW90629.1, ECO:0000313|Proteomes:UP000244011};
RN   [1] {ECO:0000313|EMBL:PTW90629.1, ECO:0000313|Proteomes:UP000244011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MWH-Ta3 {ECO:0000313|EMBL:PTW90629.1,
RC   ECO:0000313|Proteomes:UP000244011};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (APR-2018) 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}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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:PTW90629.1}.
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DR   EMBL; QBKD01000001; PTW90629.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T5X6B0; -.
DR   OrthoDB; 15218at2; -.
DR   Proteomes; UP000244011; 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:SF1; PROTEASE HTPX; 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:UP000244011};
KW   Stress response {ECO:0000313|EMBL:PTW90629.1};
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..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        37..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        189..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   DOMAIN          76..291
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   ACT_SITE        143
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         146
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         221
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   297 AA;  32178 MW;  C49DB2BA6E81F826 CRC64;
     MYSAIAANKR NTVLIIGVFL LIVVGLGWLI SQMMGDGSWS ITIATVLGAG AYAWFQYYNA
     DKIAVAMAGA QQITEQDNPR LWRTVENLTI ATGMPMPRVY IVNDPAPNAF ASGRDPEHAV
     VAATTGLLDI MTDAELEGVM AHELGHVKNY DIRVSTIVFG LVVAVGFITD ILIRMAMWGG
     GNRRNNDNGA GALFLVLGLV AMIVAPLVSA LIQAGVSRQR EYLADATGAM TTRNPEGLAS
     ALHKLAEYKA PMRRQSASMA HLWISDPMKP GVFDRMFATH PPIPERIRRL LDIGGKF
//
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