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Database: UniProt
Entry: D2TTM4_CITRI
LinkDB: D2TTM4_CITRI
Original site: D2TTM4_CITRI 
ID   D2TTM4_CITRI            Unreviewed;       572 AA.
AC   D2TTM4;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=PTS system, IIbc component {ECO:0000313|EMBL:CBG91727.1};
GN   OrderedLocusNames=ROD_50551 {ECO:0000313|EMBL:CBG91727.1};
OS   Citrobacter rodentium (strain ICC168) (Citrobacter freundii biotype 4280).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=637910 {ECO:0000313|EMBL:CBG91727.1, ECO:0000313|Proteomes:UP000001889};
RN   [1] {ECO:0000313|EMBL:CBG91727.1, ECO:0000313|Proteomes:UP000001889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ICC168 {ECO:0000313|EMBL:CBG91727.1,
RC   ECO:0000313|Proteomes:UP000001889};
RX   PubMed=19897651; DOI=10.1128/JB.01144-09;
RA   Petty N.K., Bulgin R., Crepin V.F., Cerdeno-Tarraga A.M., Schroeder G.N.,
RA   Quail M.A., Lennard N., Corton C., Barron A., Clark L., Toribio A.L.,
RA   Parkhill J., Dougan G., Frankel G., Thomson N.R.;
RT   "The Citrobacter rodentium genome sequence reveals convergent evolution
RT   with human pathogenic Escherichia coli.";
RL   J. Bacteriol. 192:525-538(2010).
CC   -!- SIMILARITY: Belongs to the four-carbon acid sugar kinase family.
CC       {ECO:0000256|ARBA:ARBA00005715}.
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DR   EMBL; FN543502; CBG91727.1; -; Genomic_DNA.
DR   RefSeq; WP_012908869.1; NC_013716.1.
DR   AlphaFoldDB; D2TTM4; -.
DR   STRING; 637910.ROD_50551; -.
DR   KEGG; cro:ROD_50551; -.
DR   eggNOG; COG3395; Bacteria.
DR   eggNOG; COG3732; Bacteria.
DR   HOGENOM; CLU_029424_0_1_6; -.
DR   OrthoDB; 4774329at2; -.
DR   Proteomes; UP000001889; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.980.20; Four-carbon acid sugar kinase, nucleotide binding domain; 1.
DR   Gene3D; 3.40.50.10840; Putative sugar-binding, N-terminal domain; 1.
DR   InterPro; IPR010737; 4-carb_acid_sugar_kinase_N.
DR   InterPro; IPR037051; 4-carb_acid_sugar_kinase_N_sf.
DR   InterPro; IPR031475; NBD_C.
DR   InterPro; IPR042213; NBD_C_sf.
DR   InterPro; IPR011618; PTS_EIIBC_GUT_N.
DR   InterPro; IPR004702; PTS_sorb_EIIBC.
DR   PANTHER; PTHR39427; -; 1.
DR   PANTHER; PTHR39427:SF1; PTS SYSTEM GLUCITOL_SORBITOL-SPECIFIC EIIB COMPONENT; 1.
DR   Pfam; PF03612; EIIBC-GUT_N; 1.
DR   Pfam; PF17042; NBD_C; 1.
DR   Pfam; PF07005; SBD_N; 1.
DR   SUPFAM; SSF142764; YgbK-like; 1.
DR   PROSITE; PS51102; PTS_EIIB_TYPE_5; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..214
FT                   /note="PTS EIIB type-5"
FT                   /evidence="ECO:0000259|PROSITE:PS51102"
FT   MOD_RES         72
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00425"
SQ   SEQUENCE   572 AA;  61510 MW;  2DA48BE690771EE8 CRC64;
     MEKHLLISKG SKGWGGPLSI NISQTKKIAY ITGGMRPPVV ERLSELTGWP SVDVFKNGEP
     PEEEIGLMVI DCGGTLRCGL YPKRGIPTIN LHPTGKSGPL AEFIHEGIYV SGVTPACIEM
     IWPQGEGGKL GIVADDLTGA TTVGVLLARS GLKTAAFFDT ESFARNEVEY PAMVVSSDSR
     PLPKAEAQHQ VSAAVKQLQA RGAHYFTKRI DTTLRGGIGF EIDAMLEQLP LETVAVVVPA
     MPQSRRILVG GYSVIDSVAL SRTDVARDVR TPVTESWVPG LLAAQTHHQV GHIALASVMK
     GEAQIQQDLQ EQQLRGVRVI VVDAITLEDV DAIAGAVIAL NWNVLAVDPG PFTERLAVRR
     GLMREAHNSA STPTTADSQR GSILIVAGSA TPVTKMQLQH LIASDDRVCH IPVDAELLVD
     RKNAAEIEVN RVVQYARQCV PAQQNTLFVF ESALTGRLLD LQEEEQRFGL ARGQAAENIN
     QGLGNIVREV LNCASGEIKG LYMTGGDTMV NVLKELGATG IEMIDYVIPQ TDMVRIIGGD
     YAGLICVGKG GLTGPQDIIS TIVERIYKEA QQ
//
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