ID Q0T044_SHIF8 Unreviewed; 481 AA.
AC Q0T044;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Suppresses inhibitory activity of CsrA {ECO:0000313|EMBL:ABF05321.1};
GN Name=tldD {ECO:0000313|EMBL:ABF05321.1};
GN OrderedLocusNames=SFV_3271 {ECO:0000313|EMBL:ABF05321.1};
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF05321.1, ECO:0000313|Proteomes:UP000000659};
RN [1] {ECO:0000313|EMBL:ABF05321.1, ECO:0000313|Proteomes:UP000000659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401 {ECO:0000313|EMBL:ABF05321.1,
RC ECO:0000313|Proteomes:UP000000659};
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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; CP000266; ABF05321.1; -; Genomic_DNA.
DR RefSeq; WP_000055909.1; NC_008258.1.
DR AlphaFoldDB; Q0T044; -.
DR SMR; Q0T044; -.
DR GeneID; 75173414; -.
DR KEGG; sfv:SFV_3271; -.
DR HOGENOM; CLU_026425_1_0_6; -.
DR Proteomes; UP000000659; 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}.
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; 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
//
