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Database: UniProt
Entry: Q0T655_SHIF8
LinkDB: Q0T655_SHIF8
Original site: Q0T655_SHIF8 
ID   Q0T655_SHIF8            Unreviewed;       726 AA.
AC   Q0T655;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Tyrosine-protein kinase etk {ECO:0008006|Google:ProtNLM};
GN   Name=yccC {ECO:0000313|EMBL:ABF03210.1};
GN   OrderedLocusNames=SFV_0990 {ECO:0000313|EMBL:ABF03210.1};
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF03210.1, ECO:0000313|Proteomes:UP000000659};
RN   [1] {ECO:0000313|EMBL:ABF03210.1, ECO:0000313|Proteomes:UP000000659}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401 {ECO:0000313|EMBL:ABF03210.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC         [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000256|ARBA:ARBA00001074};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the etk/wzc family.
CC       {ECO:0000256|ARBA:ARBA00008883}.
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DR   EMBL; CP000266; ABF03210.1; -; Genomic_DNA.
DR   RefSeq; WP_000208630.1; NC_008258.1.
DR   AlphaFoldDB; Q0T655; -.
DR   KEGG; sfv:SFV_0990; -.
DR   HOGENOM; CLU_009912_0_0_6; -.
DR   Proteomes; UP000000659; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05387; BY-kinase; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR032807; GNVR.
DR   InterPro; IPR003856; LPS_length_determ_N_term.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005702; Wzc-like_C.
DR   NCBIfam; TIGR01007; eps_fam; 1.
DR   PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR   PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR   Pfam; PF13614; AAA_31; 1.
DR   Pfam; PF13807; GNVR; 1.
DR   Pfam; PF02706; Wzz; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT   TRANSMEM        33..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..107
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          368..448
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          543..656
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          269..303
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   726 AA;  81303 MW;  AB3EDD18FC21202F CRC64;
     MTTKNMNTPP GSTQENEIDL LRLVGELWDH RKFIISVTAL FTLIAVAYSL LSTPIYQADT
     LVQVEQKQGN AILSGLSDMI PNSSPESAPE IQLLQSRMIL GKTIAELNLR DIVEQKYFPI
     VGRGWARLTK EKLGELAISW MHIPQLNGQD QQLTLTVGEN GHYTLEGEEF TVNGMVGQRL
     EKDGVALTIA DIKAKPGTQF VLSQRTELEA INALQETFTV SERSKESGML ELTMTGDDPQ
     LITRILNSIA NNYLQQNIAR QAAQDSQSLE FLQRQLPEVR SELDQAEEKL NVYRQQRDSV
     DLNLEAKAVL EQIVNVDNQL NELTFREAEI SQLYKKDHPT YRALLEKRQT LEQERKRLNK
     RVSAMPSTQQ EVLRLSRDVE AGRAVYLQLL NRQQELSISK SSAIGNVRII DPAVTQPQPV
     KPKKALNVVL GFILGLFISV SAVLARAMLR RGVEAPEQLE EHGISVYSTI PMSEWLDKRT
     RLRKKNLFSN QQRHRTKNIP FLAVDNPADS AVEAVRALRT SLHFAMMETE NNILMITGAT
     PDSGKTFVSS TLAAVIAQSD QKVLFIDADL RRGYSHNLFT VSNEHGLSEY LAGKDELNKV
     IQHFGKGGFD VITRGQVPPN PSELLMRDRM RQLLEWANDH YDLVIVDTPP MLAVSNAAVV
     GRSVGTSLLV ARFGLNTAKE VSLSMQRLEQ AGVNIKGAIL NGVIKRASTA YSYGYNYYGY
     SYSEKE
//
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