ID B7MC05_ECO45 Unreviewed; 481 AA.
AC B7MC05;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:CAR04846.1};
GN Name=tldD {ECO:0000313|EMBL:CAR04846.1};
GN OrderedLocusNames=ECS88_3620 {ECO:0000313|EMBL:CAR04846.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR04846.1, ECO:0000313|Proteomes:UP000000747};
RN [1] {ECO:0000313|Proteomes:UP000000747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928161; CAR04846.1; -; Genomic_DNA.
DR RefSeq; WP_000055911.1; NC_011742.1.
DR AlphaFoldDB; B7MC05; -.
DR KEGG; ecz:ECS88_3620; -.
DR HOGENOM; CLU_026425_1_0_6; -.
DR OMA; TDFWGSM; -.
DR Proteomes; UP000000747; 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; 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:UP000000747}.
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; 51364 MW; 4863864B0965FED1 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 GQFVFSTSEA YLIENGKVTK
PVKGATLIGS GIETMQQISM VGNDLKLDNG VGVCGKEGQS LPVGVGQPTL KVDNLTVGGT
A
//