ID A0A2U2RH04_9MICO Unreviewed; 288 AA.
AC A0A2U2RH04;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=DEO23_14830 {ECO:0000313|EMBL:PWH05134.1};
OS Brachybacterium endophyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=2182385 {ECO:0000313|EMBL:PWH05134.1, ECO:0000313|Proteomes:UP000245590};
RN [1] {ECO:0000313|EMBL:PWH05134.1, ECO:0000313|Proteomes:UP000245590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1HQ-2 {ECO:0000313|EMBL:PWH05134.1,
RC ECO:0000313|Proteomes:UP000245590};
RA Tuo L.;
RT "Brachybacterium sp. M1HQ-2T, whole genome shotgun sequence.";
RL Submitted (MAY-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:PWH05134.1}.
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DR EMBL; QFKX01000007; PWH05134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U2RH04; -.
DR OrthoDB; 15218at2; -.
DR Proteomes; UP000245590; 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; cd07336; 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:UP000245590};
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 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 33..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 144..167
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 179..200
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT DOMAIN 67..280
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 135
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 205
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ SEQUENCE 288 AA; 30884 MW; 5903B48443C25972 CRC64;
MGRSVWNILK TALLFGVLWG VLLAVGYALG GHFIWIFAII GLVGTFISFW NSDTIAIRSM
RAQEVSPQEA PQLYRIVQDL ANQAGQPMPR LYISPTQQPN AFATGRSPQR AAVCCTQGIL
QILDERELRG VLGHELMHVY NRDILTSSVA AGIAGVITSL AQMALWFGGG RDREGGGGIV
GALLAMILAP IAATLIQLAI SRTREYSADH DGADLTGDPL ALASALQKIS GGVAAHPLPK
EQNLQDSAHM MIANPFKGGG MGQLFSTHPP TEQRIARLQQ QAQQMGPR
//
