ID   TLDD_SHIFL              Reviewed;         481 AA.
AC   P0AGH0; P46473;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Metalloprotease TldD homolog;
DE            EC=3.4.-.-;
GN   Name=tldD; OrderedLocusNames=SF3283, S3499;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44747.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18558.1; -; Genomic_DNA.
DR   RefSeq; NP_709040.1; NC_004337.2.
DR   RefSeq; WP_000055909.1; NZ_WPGW01000026.1.
DR   AlphaFoldDB; P0AGH0; -.
DR   SMR; P0AGH0; -.
DR   STRING; 198214.SF3283; -.
DR   EnsemblBacteria; AAN44747; AAN44747; SF3283.
DR   EnsemblBacteria; AAP18558; AAP18558; S3499.
DR   GeneID; 1027079; -.
DR   GeneID; 66672860; -.
DR   KEGG; sfl:SF3283; -.
DR   KEGG; sfx:S3499; -.
DR   PATRIC; fig|198214.7.peg.3890; -.
DR   HOGENOM; CLU_026425_1_0_6; -.
DR   OMA; TDFWGSM; -.
DR   OrthoDB; 806701at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome.
FT   CHAIN           1..481
FT                   /note="Metalloprotease TldD homolog"
FT                   /id="PRO_0000142360"
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