ID   STEC_SALTY              Reviewed;         457 AA.
AC   Q8ZP57;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Secreted effector kinase SteC;
DE            EC=2.7.-.-;
DE   AltName: Full=Salmonella translocated effector C;
GN   Name=steC; OrderedLocusNames=STM1698;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   FUNCTION AS A KINASE, SUBCELLULAR LOCATION, SECRETION VIA TYPE III
RP   SECRETION SYSTEM, INDUCTION, AUTOPHOSPHORYLATION, AND MUTAGENESIS OF
RP   LYS-256.
RC   STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX   PubMed=17645553; DOI=10.1111/j.1462-5822.2007.01010.x;
RA   Poh J., Odendall C., Spanos A., Boyle C., Liu M., Freemont P., Holden D.W.;
RT   "SteC is a Salmonella kinase required for SPI-2-dependent F-actin
RT   remodelling.";
RL   Cell. Microbiol. 10:20-30(2008).
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. {ECO:0000269|PubMed:17645553}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17645553}. Host
CC       cytoplasm {ECO:0000269|PubMed:17645553}. Note=Secreted via type III
CC       secretion system 2 (SPI-2 TTSS), and delivered into the host cytoplasm.
CC       Localizes on or close to the Salmonella-containing vacuole (SCV)
CC       membrane, and to SPI-2-induced F-actin structures.
CC   -!- INDUCTION: Expression is regulated by the two-component regulatory
CC       system SsrA/SsrB. {ECO:0000269|PubMed:17645553}.
CC   -!- PTM: Autophosphorylated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
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DR   EMBL; AE006468; AAL20615.1; -; Genomic_DNA.
DR   RefSeq; NP_460656.1; NC_003197.2.
DR   RefSeq; WP_001116926.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZP57; -.
DR   SMR; Q8ZP57; -.
DR   STRING; 99287.STM1698; -.
DR   PaxDb; Q8ZP57; -.
DR   EnsemblBacteria; AAL20615; AAL20615; STM1698.
DR   GeneID; 1253216; -.
DR   KEGG; stm:STM1698; -.
DR   PATRIC; fig|99287.12.peg.1793; -.
DR   HOGENOM; CLU_041541_0_0_6; -.
DR   OMA; PFTFHIG; -.
DR   BioCyc; SENT99287:STM1698-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043657; C:host cell; IDA:UniProtKB.
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; IDA:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   ATP-binding; Host cytoplasm; Kinase; Nucleotide-binding;
KW   Reference proteome; Secreted; Transferase; Virulence.
FT   CHAIN           1..457
FT                   /note="Secreted effector kinase SteC"
FT                   /id="PRO_0000391639"
FT   BINDING         256
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         256
FT                   /note="K->H: Loss of kinase activity. No effect on
FT                   translocation of the protein."
FT                   /evidence="ECO:0000269|PubMed:17645553"
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