ID Q7CPM5_SALTY Unreviewed; 481 AA.
AC Q7CPM5;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Suppresses inhibitory activity of CsrA {ECO:0000313|EMBL:AAL22237.1};
GN Name=tldD {ECO:0000313|EMBL:AAL22237.1};
GN OrderedLocusNames=STM3368 {ECO:0000313|EMBL:AAL22237.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL22237.1, ECO:0000313|Proteomes:UP000001014};
RN [1] {ECO:0000313|EMBL:AAL22237.1, ECO:0000313|Proteomes:UP000001014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720
RC {ECO:0000313|Proteomes:UP000001014};
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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; AE006468; AAL22237.1; -; Genomic_DNA.
DR RefSeq; NP_462278.1; NC_003197.2.
DR RefSeq; WP_000055936.1; NC_003197.2.
DR AlphaFoldDB; Q7CPM5; -.
DR STRING; 99287.STM3368; -.
DR PaxDb; 99287-STM3368; -.
DR GeneID; 1254891; -.
DR KEGG; stm:STM3368; -.
DR PATRIC; fig|99287.12.peg.3569; -.
DR HOGENOM; CLU_026425_1_0_6; -.
DR OMA; TDFWGSM; -.
DR PhylomeDB; Q7CPM5; -.
DR BioCyc; SENT99287:STM3368-MONOMER; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IPR025502; TldD.
DR InterPro; IPR035068; TldD/PmbA_N.
DR InterPro; IPR036059; TldD/PmbA_sf.
DR PANTHER; PTHR30624:SF4; METALLOPROTEASE TLDD; 1.
DR PANTHER; PTHR30624; UNCHARACTERIZED PROTEIN TLDD AND PMBA; 1.
DR Pfam; PF01523; PmbA_TldD_1st; 1.
DR Pfam; PF19290; PmbA_TldD_2nd; 1.
DR Pfam; PF19289; PmbA_TldD_3rd; 1.
DR PIRSF; PIRSF004919; TldD; 1.
DR SUPFAM; SSF111283; Putative modulator of DNA gyrase, PmbA/TldD; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001014}.
FT DOMAIN 37..98
FT /note="Metalloprotease TldD/E N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01523"
FT DOMAIN 125..238
FT /note="Metalloprotease TldD/E central"
FT /evidence="ECO:0000259|Pfam:PF19290"
FT DOMAIN 246..479
FT /note="Metalloprotease TldD/E C-terminal"
FT /evidence="ECO:0000259|Pfam:PF19289"
SQ SEQUENCE 481 AA; 51287 MW; 8B19F4ACE23F87D4 CRC64;
MSLNLVSEQL LAANGLNHQD LFAILGQLAE RRLDYGDLYF QSSYHESWVL EDRIIKDGSY
NIDQGVGVRA ISGEKTGFAY ADQISLLALE QSAQAARTIV RENGEGKVKT LAAVAHQPLY
TTLDPLQSMS REEKLDILRR VDKAAREADK RVQEVNASLT GVYELILVAA TDGTLAADVR
PLVRLSVSVQ VEEDGKRERG ASGGGGRFGY EYFLADLDGE VRADAWAKEA VRMALVNLSA
VAAPAGTLPV VLGAGWPGVL LHEAVGHGLE GDFNRRGTSV FSGQIGEQVA SALCTVVDDG
TMMNRRGSVA IDDEGTPGQY NVLIENGVLK GYMQDKLNAR LMGAAPTGNG RRESYAHLPM
PRMTNTYMLA GQSTPQEIIE SVEYGIYAPN FGGGQVDITS GKFVFSTSEA YLIENGKVTT
PVKGATLIGS GIETMQQISM VGNDLKLDNG VGVCGKEGQS LPVGVGQPTL KVDNLTVGGT
A
//
