ID Q57GG4_SALCH Unreviewed; 473 AA.
AC Q57GG4;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Putative peptide maturation protein, maturation of antibiotic MccB17, see tld genes {ECO:0000313|EMBL:AAX68198.1};
GN Name=pmbA {ECO:0000313|EMBL:AAX68198.1};
GN OrderedLocusNames=SCH_4292 {ECO:0000313|EMBL:AAX68198.1};
OS Salmonella choleraesuis (strain SC-B67).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=321314 {ECO:0000313|EMBL:AAX68198.1, ECO:0000313|Proteomes:UP000000538};
RN [1] {ECO:0000313|EMBL:AAX68198.1, ECO:0000313|Proteomes:UP000000538}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC-B67 {ECO:0000313|EMBL:AAX68198.1,
RC ECO:0000313|Proteomes:UP000000538};
RX PubMed=15781495; DOI=10.1093/nar/gki297;
RA Chiu C.H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.Y., Wang H.S.,
RA Lee Y.S.;
RT "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT invasive and resistant zoonotic pathogen.";
RL Nucleic Acids Res. 33:1690-1698(2005).
CC -!- FUNCTION: Metalloprotease involved in CcdA degradation. Suppresses the
CC inhibitory activity of the carbon storage regulator (CsrA).
CC {ECO:0000256|ARBA:ARBA00025682}.
CC -!- SIMILARITY: Belongs to the peptidase U62 family.
CC {ECO:0000256|ARBA:ARBA00005836}.
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DR EMBL; AE017220; AAX68198.1; -; Genomic_DNA.
DR AlphaFoldDB; Q57GG4; -.
DR KEGG; sec:SCH_4292; -.
DR HOGENOM; CLU_026425_0_0_6; -.
DR Proteomes; UP000000538; Chromosome.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2290.10; PmbA/TldD superfamily; 1.
DR InterPro; IPR045569; Metalloprtase-TldD/E_C.
DR InterPro; IPR045570; Metalloprtase-TldD/E_cen_dom.
DR InterPro; IPR002510; Metalloprtase-TldD/E_N.
DR InterPro; IPR047657; PmbA.
DR InterPro; IPR035068; TldD/PmbA_N.
DR InterPro; IPR036059; TldD/PmbA_sf.
DR PANTHER; PTHR43421; METALLOPROTEASE PMBA; 1.
DR PANTHER; PTHR43421:SF1; METALLOPROTEASE PMBA; 1.
DR Pfam; PF01523; PmbA_TldD_1st; 1.
DR Pfam; PF19290; PmbA_TldD_2nd; 1.
DR Pfam; PF19289; PmbA_TldD_3rd; 1.
DR SUPFAM; SSF111283; Putative modulator of DNA gyrase, PmbA/TldD; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Protease {ECO:0000256|ARBA:ARBA00022670}.
FT DOMAIN 59..123
FT /note="Metalloprotease TldD/E N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01523"
FT DOMAIN 151..257
FT /note="Metalloprotease TldD/E central"
FT /evidence="ECO:0000259|Pfam:PF19290"
FT DOMAIN 265..472
FT /note="Metalloprotease TldD/E C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19289"
SQ SEQUENCE 473 AA; 51257 MW; 5434B38337CFD27A CRC64;
MLPVKMRTEK RFSVRLQRNS LYIMAFAMKV ISQVEAQRKI LEEAVSTALE LASGKSDGAE
VAVSKTTGIS VSTRYGEVEN VEFNSDGALG ITVYHQNRKG SASSTDLSPQ AIARTVQAAL
DIARYTSPDP CAGVADKELL AFDAPDLDLF HPAEVTPDEA IELAARAEQA SLKADKRITN
TEGGSFNSHY GIKVFGNSHG MLQGYCSTRH SLSSCVIAEE NGDMERDYAY TIGRAMADLQ
APEWVGAECA RRTLSRLSPR KLSTMKAPVI FANEVATGLF GHLVGAIAGG AVYRKSTFLL
DSLGKQILPE WLTIEEHPHL LKGLASSPFD SEGVRTERRD IVKDGVLTQW LLTNYSARKL
GLKSTGHAGG IHNWRIAGQG LNFEQLLKEM GTGLVVTELM GQGVSGITGD YSRGAAGFWV
ENGEIQYPVS EITIAGNLKE MWRNIVTVGD DIETRSNIQC GSVLLPEMKI AGQ
//
