ID D7BU43_STRBB Unreviewed; 413 AA.
AC D7BU43;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN OrderedLocusNames=SBI_08474 {ECO:0000313|EMBL:ADI11592.1};
OS Streptomyces bingchenggensis (strain BCW-1).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI11592.1, ECO:0000313|Proteomes:UP000000377};
RN [1] {ECO:0000313|EMBL:ADI11592.1, ECO:0000313|Proteomes:UP000000377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCW-1 {ECO:0000313|EMBL:ADI11592.1,
RC ECO:0000313|Proteomes:UP000000377};
RX PubMed=20581206; DOI=10.1128/JB.00596-10;
RA Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA Xiang W.S.;
RT "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT bingchenggensis.";
RL J. Bacteriol. 192:4526-4527(2010).
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; CP002047; ADI11592.1; -; Genomic_DNA.
DR RefSeq; WP_014181041.1; NC_016582.1.
DR AlphaFoldDB; D7BU43; -.
DR STRING; 749414.SBI_08474; -.
DR KEGG; sbh:SBI_08474; -.
DR PATRIC; fig|749414.3.peg.8721; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG1994; Bacteria.
DR HOGENOM; CLU_037123_1_0_11; -.
DR Proteomes; UP000000377; 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; cd02205; CBS_pair_SF; 1.
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.
PE 3: Inferred from homology;
KW CBS domain {ECO:0000256|ARBA:ARBA00023122};
KW 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:UP000000377};
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 43..63
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 135..158
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 164..188
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT TRANSMEM 251..272
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT DOMAIN 83..159
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 169..224
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 290..335
FT /note="CBS"
FT /evidence="ECO:0000259|Pfam:PF00571"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ SEQUENCE 413 AA; 43916 MW; 795256F745FC4840 CRC64;
MDNSGQRQSD SGGSDRTTEP EGEKPQRPRE TGGGFLMGRP FGVPVYVSPS WFLVAALITW
VFGGQLERVL PELGAARYIV SLFFAVAFYA SVLVHELAHT VAALRFKLPV RRIQLQFFGG
VSEIEKESET PGREFVLAFV GPLLSLILSG LFYLGMLFVE PDTVVGVLLA GLMISNLIVA
AFNLLPGLPL DGGRMLRAVV WKISGKPMTG TVAAAWTGRA LAVAVLVGLP LATQTGGFGD
EAEGFGSVDS LTDALLAAIL AAIIWTGAGN SLRMARLRER LPDLRARTLT RRAVPVAADT
PLSEALRRAN EAGARALVVV DGQGAPTAVV REAAIVGVPE HRRPWVAVSG LAQDLKEGMR
VSAELTGEEL LDTLRATPAT EYLVVEDTGE IYGVLSTADV ERAFVAAMAR TPS
//
