TLDD_ECOL6
ID TLDD_ECOL6 Reviewed; 481 AA.
AC P0AGG9; P46473;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Metalloprotease TldD;
DE EC=3.4.-.-;
GN Name=tldD; OrderedLocusNames=c3999;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Metalloprotease involved in CcdA degradation. Suppresses the
CC inhibitory activity of the carbon storage regulator (CsrA) (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase U62 family. {ECO:0000305}.
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DR EMBL; AE014075; AAN82439.1; -; Genomic_DNA.
DR RefSeq; WP_000055909.1; NC_004431.1.
DR AlphaFoldDB; P0AGG9; -.
DR SMR; P0AGG9; -.
DR STRING; 199310.c3999; -.
DR EnsemblBacteria; AAN82439; AAN82439; c3999.
DR GeneID; 66672860; -.
DR KEGG; ecc:c3999; -.
DR eggNOG; COG0312; Bacteria.
DR HOGENOM; CLU_026425_1_0_6; -.
DR OMA; TDFWGSM; -.
DR BioCyc; ECOL199310:C3999-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.30.2290.10; -; 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 Pfam; PF01523; PmbA_TldD; 1.
DR Pfam; PF19289; PmbA_TldD_C; 1.
DR Pfam; PF19290; PmbA_TldD_M; 1.
DR PIRSF; PIRSF004919; TldD; 1.
DR SUPFAM; SSF111283; SSF111283; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metalloprotease; Protease.
FT CHAIN 1..481
FT /note="Metalloprotease TldD"
FT /id="PRO_0000142358"
SQ SEQUENCE 481 AA; 51364 MW; C2D9F681B305FECD CRC64;
MSLNLVSEQL LAANGLKHQD LFAILGQLAE RRLDYGDLYF QSSYHESWVL EDRIIKDGSY
NIDQGVGVRA ISGEKTGFAY ADQISLLALE QSAQAARTIV RDSGDGKVQT LGAVEHSPLY
TSVDPLQSMS REEKLDILRR VDKVAREADK RVQEVTASLS GVYELILVAA TDGTLAADVR
PLVRLSVSVL VEEDGKRERG ASGGGGRFGY EFFLADLDGE VRADAWAKEA VRMALVNLSA
VAAPAGTMPV VLGAGWPGVL LHEAVGHGLE GDFNRRGTSV FSGQVGELVA SELCTVVDDG
TMVDRRGSVA IDDEGTPGQY NVLIENGILK GYMQDKLNAR LMGMTPTGNG RRESYAHLPM
PRMTNTYMLP GKSTPQEIIE SVEYGIYAPN FGGGQVDITS GKFVFSTSEA YLIENGKVTK
PVKGATLIGS GIETMQQISM VGNDLKLDNG VGVCGKEGQS LPVGVGQPTL KVDNLTVGGT
A