TLDD_ECOLI
ID TLDD_ECOLI Reviewed; 481 AA.
AC P0AGG8; P46473; Q2M8W9;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Metalloprotease TldD;
DE EC=3.4.-.-;
GN Name=tldD; Synonyms=yhdO; OrderedLocusNames=b3244, JW3213;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=8604133; DOI=10.1006/jmbi.1996.0103;
RA Murayama N., Shimizu H., Takiguchi S., Baba Y., Amino H., Horiuchi T.,
RA Sekimizu K., Miki T.;
RT "Evidence for involvement of Escherichia coli genes pmbA, csrA and a
RT previously unrecognized gene tldD, in the control of DNA gyrase by letD
RT (ccdB) of sex factor F.";
RL J. Mol. Biol. 256:483-502(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=12029038; DOI=10.1128/jb.184.12.3224-3231.2002;
RA Allali N., Afif H., Couturier M., Van Melderen L.;
RT "The highly conserved TldD and TldE proteins of Escherichia coli are
RT involved in microcin B17 processing and in CcdA degradation.";
RL J. Bacteriol. 184:3224-3231(2002).
CC -!- FUNCTION: Metalloprotease involved in CcdA degradation. Suppresses the
CC inhibitory activity of the carbon storage regulator (CsrA).
CC {ECO:0000269|PubMed:12029038}.
CC -!- MISCELLANEOUS: In strains containing the pMccB17 plasmid, required for
CC the maturation and secretion of the antibiotic bacteriocin microcin B17
CC (MccB17). {ECO:0000305|PubMed:12029038}.
CC -!- SIMILARITY: Belongs to the peptidase U62 family. {ECO:0000305}.
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DR EMBL; D44451; BAA07913.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58046.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76276.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77287.1; -; Genomic_DNA.
DR PIR; F65116; F65116.
DR RefSeq; NP_417711.1; NC_000913.3.
DR RefSeq; WP_000055909.1; NZ_STEB01000012.1.
DR PDB; 5NJ5; X-ray; 1.90 A; A/C=1-481.
DR PDB; 5NJ9; X-ray; 1.25 A; A/C=1-481.
DR PDB; 5NJA; X-ray; 1.40 A; A/C=1-481.
DR PDB; 5NJB; X-ray; 1.50 A; A/C=1-481.
DR PDB; 5NJC; X-ray; 1.35 A; A/C=1-481.
DR PDB; 5NJF; X-ray; 1.42 A; A/C=1-481.
DR PDBsum; 5NJ5; -.
DR PDBsum; 5NJ9; -.
DR PDBsum; 5NJA; -.
DR PDBsum; 5NJB; -.
DR PDBsum; 5NJC; -.
DR PDBsum; 5NJF; -.
DR AlphaFoldDB; P0AGG8; -.
DR SMR; P0AGG8; -.
DR BioGRID; 4260797; 17.
DR DIP; DIP-47845N; -.
DR IntAct; P0AGG8; 4.
DR STRING; 511145.b3244; -.
DR jPOST; P0AGG8; -.
DR PaxDb; P0AGG8; -.
DR PRIDE; P0AGG8; -.
DR EnsemblBacteria; AAC76276; AAC76276; b3244.
DR EnsemblBacteria; BAE77287; BAE77287; BAE77287.
DR GeneID; 66672860; -.
DR GeneID; 947749; -.
DR KEGG; ecj:JW3213; -.
DR KEGG; eco:b3244; -.
DR PATRIC; fig|1411691.4.peg.3484; -.
DR EchoBASE; EB2677; -.
DR eggNOG; COG0312; Bacteria.
DR HOGENOM; CLU_026425_1_0_6; -.
DR InParanoid; P0AGG8; -.
DR OMA; TDFWGSM; -.
DR PhylomeDB; P0AGG8; -.
DR BioCyc; EcoCyc:G7689-MON; -.
DR BioCyc; MetaCyc:76890-MON; -.
DR PRO; PR:P0AGG8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:1905368; C:peptidase complex; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0016485; P:protein processing; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metalloprotease; Protease; Reference proteome.
FT CHAIN 1..481
FT /note="Metalloprotease TldD"
FT /id="PRO_0000142357"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 18..29
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 34..51
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 54..72
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 75..83
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:5NJ9"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 131..148
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 152..170
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 173..193
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 196..208
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 222..239
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:5NJ9"
FT TURN 280..283
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 320..325
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 364..368
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 375..380
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 383..397
FT /evidence="ECO:0007829|PDB:5NJ9"
FT TURN 398..401
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 402..414
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 417..422
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:5NJ9"
FT HELIX 431..436
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 452..456
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 459..467
FT /evidence="ECO:0007829|PDB:5NJ9"
FT STRAND 470..478
FT /evidence="ECO:0007829|PDB:5NJ9"
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
