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Database: UniProt
Entry: A0A344U9A2_9ACTN
LinkDB: A0A344U9A2_9ACTN
Original site: A0A344U9A2_9ACTN 
ID   A0A344U9A2_9ACTN        Unreviewed;       379 AA.
AC   A0A344U9A2;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN   ORFNames=C0216_12830 {ECO:0000313|EMBL:AXE27473.1};
OS   Streptomyces globosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68209 {ECO:0000313|EMBL:AXE27473.1, ECO:0000313|Proteomes:UP000252004};
RN   [1] {ECO:0000313|EMBL:AXE27473.1, ECO:0000313|Proteomes:UP000252004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LZH-48 {ECO:0000313|EMBL:AXE27473.1,
RC   ECO:0000313|Proteomes:UP000252004};
RA   Ran K., Li Z., Wei S., Dong R.;
RT   "Draft genome Sequence of streptomyces globosus LZH-48.";
RL   Submitted (JAN-2018) 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; CP030862; AXE27473.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A344U9A2; -.
DR   KEGG; sgz:C0216_12830; -.
DR   OrthoDB; 9781963at2; -.
DR   Proteomes; UP000252004; 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; 2.
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:UP000252004};
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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        45..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        114..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        142..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        185..208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        214..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   DOMAIN          251..309
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        67
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         165
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ   SEQUENCE   379 AA;  39006 MW;  391EAF3207B257F9 CRC64;
     MKPTFSLGTI AGVRVGVHWS VLVIVAVIAL VLSGRLPAAH PGRPGWQYAV TTLVAAAFLL
     LSLLAHELSH AVVARRNGVA VGDITLWLLG GMARLGGEPP TPGAEARIAG VGPLVSLLLG
     LLFGLLAGAA AAALGAGLAV EALAWLGGIN VLLAVFNALP AAPLDGGRLL RAVVWRRTGD
     RLRATAVATG ASRLLGWALV AVGLLLVLRG VPLSGIWIVL VGWFLVAVAT AEGSQAKLEE
     LLSGVTVGEA MGRDPVTVPA SLAVGRFLAA PQFRFRHSAF PVVDADRRPV GLVSVNAAAR
     VPEERHGTTR VADVMIPIEE VPTPHPGDPL TGVLPVLESS PAHRAVVLAG GAVVGVVTSS
     DVSRVTSWLA SSRWRKRAV
//
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