ID J7Q5E2_METSZ Unreviewed; 370 AA.
AC J7Q5E2;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN OrderedLocusNames=BN69_3498 {ECO:0000313|EMBL:CCJ08949.1};
OS Methylocystis sp. (strain SC2).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylocystaceae; Methylocystis.
OX NCBI_TaxID=187303 {ECO:0000313|EMBL:CCJ08949.1, ECO:0000313|Proteomes:UP000005263};
RN [1] {ECO:0000313|EMBL:CCJ08949.1, ECO:0000313|Proteomes:UP000005263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:CCJ08949.1,
RC ECO:0000313|Proteomes:UP000005263};
RX PubMed=23045511; DOI=10.1128/JB.01446-12;
RA Dam B., Dam S., Kube M., Reinhardt R., Liesack W.;
RT "Complete Genome Sequence of Methylocystis sp. Strain SC2, an Aerobic
RT Methanotroph with High-Affinity Methane Oxidation Potential.";
RL J. Bacteriol. 194:6008-6009(2012).
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; HE956757; CCJ08949.1; -; Genomic_DNA.
DR RefSeq; WP_014892975.1; NC_018485.1.
DR AlphaFoldDB; J7Q5E2; -.
DR STRING; 187303.BN69_3498; -.
DR KEGG; msc:BN69_3498; -.
DR PATRIC; fig|187303.17.peg.3777; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG1994; Bacteria.
DR HOGENOM; CLU_037123_1_1_5; -.
DR OrthoDB; 9781963at2; -.
DR Proteomes; UP000005263; Chromosome.
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 SMART; SM00116; 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 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 15..33
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 45..63
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 98..121
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 141..159
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 189..215
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 237..296
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 370 AA; 39776 MW; 64AFDE6B6AB2EB5A CRC64;
MRWSLTIGSF MGTAVRIHVT FLLLLGWIGF AAYQRGGAVA ARDSVLFIVA IFICVVLHEF
GHILTARRYG IVSPVITLLP IGGVADMEKM PDKPRQELLI ALAGPAVNLV IAAALILFLG
AVDVSDGIQI SDPSVNLLKR LAAVNIFLAA FNLIPAFPMD GGRVLRAALS IWIGKGRATR
IAAQIGQGFA FLLGFIGLFG NPLLLFIAIF VYIAAAGEAQ MTSMSEAARG LRAADAMETR
IAVIERGASV REAVDILLAT SQDEFPVVDG SRRLNGFLSR TNIIEALRAS EPGAPIAPFV
RQEPETIDGR ESIDAVLPKL TGGETVGVTD EEGRFLGLLT RQSLAEIMMI KDVRPDWRFS
PRDDSRPTVA
//
