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Database: UniProt
Entry: A0A1C5JXW2_9ACTN
LinkDB: A0A1C5JXW2_9ACTN
Original site: A0A1C5JXW2_9ACTN 
ID   A0A1C5JXW2_9ACTN        Unreviewed;       384 AA.
AC   A0A1C5JXW2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN   ORFNames=GA0070614_5670 {ECO:0000313|EMBL:SCG75424.1};
OS   Micromonospora coxensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=356852 {ECO:0000313|EMBL:SCG75424.1, ECO:0000313|Proteomes:UP000198215};
RN   [1] {ECO:0000313|EMBL:SCG75424.1, ECO:0000313|Proteomes:UP000198215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45161 {ECO:0000313|EMBL:SCG75424.1,
RC   ECO:0000313|Proteomes:UP000198215};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006404,
CC         ECO:0000256|PIRSR:PIRSR006404-2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRNR:PIRNR006404,
CC       ECO:0000256|PIRSR:PIRSR006404-2};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
CC       Multi-pass membrane protein {ECO:0000256|PIRNR:PIRNR006404}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|PIRNR:PIRNR006404}.
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DR   EMBL; LT607753; SCG75424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5JXW2; -.
DR   Proteomes; UP000198215; Chromosome i.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06164; S2P-M50_SpoIVFB_CBS; 1.
DR   InterPro; IPR008915; Peptidase_M50.
DR   InterPro; IPR016483; UCP006404_Pept_M50_CBS.
DR   PANTHER; PTHR39188; MEMBRANE-ASSOCIATED ZINC METALLOPROTEASE M50B; 1.
DR   PANTHER; PTHR39188:SF3; ZINC METALLOPROTEASE SLR1821-RELATED; 1.
DR   Pfam; PF02163; Peptidase_M50; 2.
DR   PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122};
KW   Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006404};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006404};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006404,
KW   ECO:0000256|PIRSR:PIRSR006404-2};
KW   Metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
KW   Protease {ECO:0000256|PIRNR:PIRNR006404, ECO:0000313|EMBL:SCG75424.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|PIRNR:PIRNR006404};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|PIRNR:PIRNR006404};
KW   Zinc {ECO:0000256|PIRNR:PIRNR006404, ECO:0000256|PIRSR:PIRSR006404-2}.
FT   TRANSMEM        21..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        117..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        146..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        195..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        220..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   DOMAIN          66..141
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   DOMAIN          151..203
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
FT   ACT_SITE        78
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         173
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ   SEQUENCE   384 AA;  40261 MW;  36589B78DF111411 CRC64;
     MNSPTPAPRR AGRRAGLTVG RVFGVPLRVD VSMLLLTLLI TVMYAQFARD RLDLPPLGGY
     LIGLGFVVSL LGSVLLHELG HALTARRHGI GVRGITLELL GGYTEMDSDA PSPRVELLVS
     LAGPAVSAVL GAVGVGLTLA LPAGTLAHQL ALQLALSNVV VAIFNLLPGL PLDGGRALRA
     AVWAATRDRH RATEVAGWVG RAVAVGTAGL VVLLTVERLL VPLALPLMLL VAVTLWRGAG
     QSIRYARISR RVPSIDLARL TRPVFGVPTG TPLAEAQRRH AEQAPPGAAV TVLDSTGRTL
     ALLDPAAADA VPVPRRPWLA VDAVARPLAQ LPTLPAGLDG ERVLEVVQAH PAARYVVTAG
     EDVVGVLHIA DLAQVLEPTR KMNR
//
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