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Database: UniProt
Entry: A0A344U9U0_9ACTN
LinkDB: A0A344U9U0_9ACTN
Original site: A0A344U9U0_9ACTN 
ID   A0A344U9U0_9ACTN        Unreviewed;       377 AA.
AC   A0A344U9U0;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|PIRNR:PIRNR006404};
GN   ORFNames=C0216_21660 {ECO:0000313|EMBL:AXE27661.1};
OS   Streptomyces globosus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=68209 {ECO:0000313|EMBL:AXE27661.1, ECO:0000313|Proteomes:UP000252004};
RN   [1] {ECO:0000313|EMBL:AXE27661.1, ECO:0000313|Proteomes:UP000252004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LZH-48 {ECO:0000313|EMBL:AXE27661.1,
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; AXE27661.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A344U9U0; -.
DR   KEGG; sgz:C0216_21660; -.
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   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        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        46..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        131..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        173..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   TRANSMEM        209..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|PIRNR:PIRNR006404"
FT   DOMAIN          253..312
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   ACT_SITE        60
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-1"
FT   BINDING         59
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         63
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
FT   BINDING         155
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006404-2"
SQ   SEQUENCE   377 AA;  40074 MW;  BA8351D11B852E7E CRC64;
     MGRPFGVPVY VSPSWFLVAA LITWVFGDQL DRVLPDLGPA RYLVSLFFAV AFYGSVLVHE
     LAHTVAALRF RLPVRRIQLQ FFGGVSEIEK ESETPGREFV LAFVGPLLSL LLAGAFYLGM
     NAVEAGTVPG VLLAGLMISN LLVAAFNLLP GLPLDGGRML RAVIWGITGK PMAGTVAAAW
     VGRGLAVAVL LGLPMITHTG LLGAPGEEAG GMSTVMDALL AAILAAIIWT GAGNSLRMAR
     LREHLPQLRA RALTRRAVPV EHATPLSEAL RRANAHGARA IVVVDGQGEP HAIVRESAIA
     SVPEHRRPWV AVSSLAQDLT DGMKVSAELA GEELLERLRS TPATEYLVVE AGGEVYGVLS
     TLDVEKAFVK AMARPRP
//
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