ID   A0A5Q0S7R6_9PSED        Unreviewed;       400 AA.
AC   A0A5Q0S7R6;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=M48 family metalloprotease {ECO:0000313|EMBL:QGA50125.1};
GN   ORFNames=GFU70_13630 {ECO:0000313|EMBL:QGA50125.1};
OS   Pseudomonas brassicacearum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=930166 {ECO:0000313|EMBL:QGA50125.1, ECO:0000313|Proteomes:UP000329489};
RN   [1] {ECO:0000313|EMBL:QGA50125.1, ECO:0000313|Proteomes:UP000329489}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S-1 {ECO:0000313|EMBL:QGA50125.1,
RC   ECO:0000313|Proteomes:UP000329489};
RA   Mandryk-Litvinkovich M.N., Muratova A., Nosonova T.L., Evdokimova O.V.,
RA   Valentovich L.N., Titok M.A., Kolomiets E.I.;
RT   "Molecular genetic analysis of determinants defining synthesis of 2,4-
RT   diacetylphloroglucinol by Pseudomonas brassicacearum BIM B-446 bacteria.";
RL   Prikl. Biokhim. Mikrobiol. 53:31-39(2017).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003983};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|RuleBase:RU003983};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M48 family.
CC       {ECO:0000256|RuleBase:RU003983}.
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DR   EMBL; CP045701; QGA50125.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5Q0S7R6; -.
DR   Proteomes; UP000329489; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR   PANTHER; PTHR43221:SF1; PROTEASE HTPX; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003983};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003983};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003983};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003983}.
FT   DOMAIN          92..244
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
SQ   SEQUENCE   400 AA;  44909 MW;  5361FEF4A2D626A9 CRC64;
     MSNPALDISS LTPLPYHQQV VNYLKTSEPA VWSWASSLGV QQEHAQEVRA QLLRDTYRLH
     PDTHPDAYQA CETALQRLHI QAPATLYQAG DGGMNASLYY LAGEVHVVFY GPILERLDAQ
     ELLALLGHEL AHYRLWSEHD GDYLTAERIL NHTLADVYTP ASLEQTARLY SLHTEIYADR
     GAALVASGPE AAITTLVKVH TGIVTVNAAS YLQQAKELDG NDAQLSRGVS HPETFLRSQA
     LDSWWQQIPD IDAWLHRRLR GPLSLNRLDV TDQVELTALT RRFIASFIKA PALQSEAVGN
     QVCGFFPDWK DTETPLDLST LDVERIDASI HEYLHFIMLD LCLVDRDLRD DALLHAARTA
     KKLGSADDFI NVLKRDIKLP KRELDPLIRA LKAEVDTWTQ
//