ID A0A2V2PRV3_9ACTN Unreviewed; 287 AA.
AC A0A2V2PRV3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=DKT74_30355 {ECO:0000313|EMBL:PWS40905.1};
OS Streptomyces sp. ZEA17I.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2202516 {ECO:0000313|EMBL:PWS40905.1, ECO:0000313|Proteomes:UP000245984};
RN [1] {ECO:0000313|EMBL:PWS40905.1, ECO:0000313|Proteomes:UP000245984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZEA17I {ECO:0000313|EMBL:PWS40905.1,
RC ECO:0000313|Proteomes:UP000245984};
RA Chen X., Qin K., Li H., Cortesi P., Saracchi M., Sang W., Yang M.;
RT "Genome sequencing and identification of chitinase family genes of
RT Streptomyces sp. ZEA17I, a biocontrol agent against plant pathogens.";
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:PWS40905.1}.
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DR EMBL; QGMS01001556; PWS40905.1; -; Genomic_DNA.
DR RefSeq; WP_018490771.1; NZ_QGMS01001556.1.
DR AlphaFoldDB; A0A2V2PRV3; -.
DR Proteomes; UP000245984; 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 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 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..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 143..166
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT DOMAIN 68..282
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 134
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT BINDING 137
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 287 AA; 31050 MW; 472EE21B1EC78B66 CRC64;
MHRRHNGLKT AVLLGGLSAL IIIIGSFFGR TGLVVALVVA VGTNAYAYWN SDKLALRAMR
ARPVSEFEAP QIYRIVRELS TAARQPMPRL YISPTQAPNA FATGRNPRNA AVCCTEGILQ
ILDERELRGV LGHELSHVYN RDILISSVAG ALASVVMFLV NFAWLIPIGR SNDDEGPGLL
GMLLIMILGP LAASVIQLAV SRSREYEADA SGAQLTGDPL ALASALRKLD AGTKQLPLPP
EPKIETASHM MIANPFRPGQ GMAKMFSTHP PMAERIARLE QMAGRRP
//
