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Database: UniProt
Entry: A0A1B1PKJ5_9RHOB
LinkDB: A0A1B1PKJ5_9RHOB
Original site: A0A1B1PKJ5_9RHOB 
ID   A0A1B1PKJ5_9RHOB        Unreviewed;       357 AA.
AC   A0A1B1PKJ5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN   ORFNames=AYJ57_01275 {ECO:0000313|EMBL:ANT59107.1};
OS   Salipiger sp. CCB-MM3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1792508 {ECO:0000313|EMBL:ANT59107.1, ECO:0000313|Proteomes:UP000092483};
RN   [1] {ECO:0000313|EMBL:ANT59107.1, ECO:0000313|Proteomes:UP000092483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB-MM3 {ECO:0000313|EMBL:ANT59107.1,
RC   ECO:0000313|Proteomes:UP000092483};
RA   Lau N.-S., Sam K.K., Abdullah A.A.-A., Chong A.S.-C.;
RT   "Genome feautures of moderately halophilic polyhydroxyalkanoate-producing
RT   Yangia sp. CCB-MM3.";
RL   Submitted (FEB-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; CP014595; ANT59107.1; -; Genomic_DNA.
DR   RefSeq; WP_066100080.1; NZ_CP014595.1.
DR   AlphaFoldDB; A0A1B1PKJ5; -.
DR   STRING; 1792508.AYJ57_01275; -.
DR   KEGG; yan:AYJ57_01275; -.
DR   OrthoDB; 9781963at2; -.
DR   Proteomes; UP000092483; Chromosome 1.
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   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
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; PF00571; CBS; 1.
DR   Pfam; PF02163; Peptidase_M50; 2.
DR   PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   PROSITE; PS51371; CBS; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; Cell membrane {ECO:0000256|PIRNR:PIRNR006404};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR006404};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006404};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR006404};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|PIRNR:PIRNR006404};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR006404};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092483};
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|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006404}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        45..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        98..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        136..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        188..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   DOMAIN          238..294
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT   BINDING         58
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ   SEQUENCE   357 AA;  37659 MW;  70E955CBD599CDE0 CRC64;
     MSWSFPIGRL FGSELRVHAT FFLLLLWIGA AAWSVGGAAA AVQNILFILA LFACVVAHEF
     GHALTARRFG IKTPDITLLP IGGLARLERM PENPVQEILV ALAGPMVNVV IWLVLVLLGA
     SSGFGGLEGL GTGTGAFLGQ LAAINLALAL FNMIPAFPMD GGRVLRAVLA LRIGRVKATQ
     AAATTGQILA FGLAFWGLSS GNFILILIAI FVFFAGQAES QDVASRAVAH DLLARDAMIT
     SFEALRPEDT LAMAGQTLIR TTQHEFPVLA PSGELAGFLT RDALFRGMAE DHAARQVSEL
     MTEVPQLPLA APLQSVLDAL AQAPAVAVID AQSRVLGYVT RENVGELMVL RGPGMTG
//
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