STEC_SALT1
ID STEC_SALT1 Reviewed; 457 AA.
AC D0ZIB5;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Secreted effector kinase SteC;
DE EC=2.7.-.-;
DE AltName: Full=Salmonella translocated effector C;
GN Name=steC; OrderedLocusNames=STM14_2050;
OS Salmonella typhimurium (strain 14028s / SGSC 2262).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=588858;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14028s / SGSC 2262;
RX PubMed=19897643; DOI=10.1128/jb.01233-09;
RA Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT "Short-term signatures of evolutionary change in the Salmonella enterica
RT serovar typhimurium 14028 genome.";
RL J. Bacteriol. 192:560-567(2010).
RN [2]
RP SUBCELLULAR LOCATION, AND SECRETION VIA TYPE III SECRETION SYSTEM.
RX PubMed=16177297; DOI=10.1128/iai.73.10.6260-6271.2005;
RA Geddes K., Worley M., Niemann G., Heffron F.;
RT "Identification of new secreted effectors in Salmonella enterica serovar
RT Typhimurium.";
RL Infect. Immun. 73:6260-6271(2005).
CC -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC promote bacterial survival in host tissues. This protein is a kinase,
CC which is required for SPI-2 TTSS-dependent F-actin meshwork formation
CC in infected host cells (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC D0ZIB5; O95466: FMNL1; Xeno; NbExp=6; IntAct=EBI-27033646, EBI-720020;
CC D0ZIB5; Q9JL26: Fmnl1; Xeno; NbExp=6; IntAct=EBI-27033646, EBI-772250;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16177297}. Host
CC cytoplasm {ECO:0000269|PubMed:16177297}. Note=Secreted via type III
CC secretion system 2 (SPI-2 TTSS), and delivered into the host cytoplasm.
CC -!- PTM: Autophosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR EMBL; CP001363; ACY88518.1; -; Genomic_DNA.
DR RefSeq; WP_001116926.1; NZ_CP043402.1.
DR AlphaFoldDB; D0ZIB5; -.
DR SMR; D0ZIB5; -.
DR IntAct; D0ZIB5; 72.
DR MINT; D0ZIB5; -.
DR EnsemblBacteria; ACY88518; ACY88518; STM14_2050.
DR KEGG; seo:STM14_2050; -.
DR PATRIC; fig|588858.6.peg.1940; -.
DR HOGENOM; CLU_041541_0_0_6; -.
DR OMA; PFTFHIG; -.
DR BioCyc; SENT588858:STM14_RS09380-MON; -.
DR PHI-base; PHI:3772; -.
DR Proteomes; UP000002695; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW ATP-binding; Host cytoplasm; Kinase; Nucleotide-binding; Secreted;
KW Transferase; Virulence.
FT CHAIN 1..457
FT /note="Secreted effector kinase SteC"
FT /id="PRO_0000391640"
FT BINDING 256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 457 AA; 52302 MW; 287CD1B6C02B5ECB CRC64;
MPFTFQIGNH SCQISERYLR DIIDNKREHV FSTCEKFIDF FRNIFTRRSL ISDYREIYNL
LCQKKEHPDI KGPFSPGPFS KRDEDCTRWR PLLGYIKLID ASRPETIDKY TVEVLAHQEN
MLLLQMFYDG VLVTETECSE RCVDFLKETM FNYNNGEITL AALGNDNLPP SEAGSNGIYE
AFEQRLIDFL TTPATASGYE SGAIDQTDAS QPAAIEAFIN SPEFQKNIRM RDIEKNKIGS
GSYGTVYRLH DDFVVKIPVN ERGIKVDVNS PEHRNCHPDR VSKYLNMAND DKNFSRSAIM
NINGKDVTVL VSKYIQGQEF DVEDEDNYRM AEALLKSRGV YMHDINILGN ILVKEGVLFF
VDGDQIVLSQ ESRQQRSVSL ATRQLEEQIK AHHMIKLKRA ETEGNTEDVE YYKSLITDLD
ALIGEEEQTP APGRRFKLAA PEEGTLVAKV LKDELKK
