PGTB_SALTY
ID PGTB_SALTY Reviewed; 668 AA.
AC P37433;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Phosphoglycerate transport system sensor protein PgtB;
DE EC=2.7.13.3;
GN Name=pgtB; OrderedLocusNames=STM2397;
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 [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=2842311; DOI=10.1128/jb.170.9.4299-4303.1988;
RA Yang Y.L., Goldrick D., Hong J.-S.;
RT "Identification of the products and nucleotide sequences of two regulatory
RT genes involved in the exogenous induction of phosphoglycerate transport in
RT Salmonella typhimurium.";
RL J. Bacteriol. 170:4299-4303(1988).
RN [2]
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 [3]
RP CHARACTERIZATION.
RX PubMed=2842312; DOI=10.1128/jb.170.9.4304-4308.1988;
RA Jiang S.Q., Yu G.Q., Li Z.G., Hong J.-S.;
RT "Genetic evidence for modulation of the activator by two regulatory
RT proteins involved in the exogenous induction of phosphoglycerate transport
RT in Salmonella typhimurium.";
RL J. Bacteriol. 170:4304-4308(1988).
CC -!- FUNCTION: Member of the two-component regulatory system PgtB/PgtA that
CC regulates the inducible phosphoglycerate transport system. Activates
CC PgtA by phosphorylation.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
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DR EMBL; M21279; AAA68215.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21297.1; -; Genomic_DNA.
DR PIR; T11778; T11778.
DR RefSeq; NP_461338.1; NC_003197.2.
DR RefSeq; WP_000678496.1; NC_003197.2.
DR AlphaFoldDB; P37433; -.
DR SMR; P37433; -.
DR STRING; 99287.STM2397; -.
DR PaxDb; P37433; -.
DR EnsemblBacteria; AAL21297; AAL21297; STM2397.
DR GeneID; 1253919; -.
DR KEGG; stm:STM2397; -.
DR PATRIC; fig|99287.12.peg.2535; -.
DR HOGENOM; CLU_020981_1_0_6; -.
DR OMA; NAMSTYL; -.
DR PhylomeDB; P37433; -.
DR BioCyc; SENT99287:STM2397-MON; -.
DR BRENDA; 2.7.13.3; 5542.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR017116; Sig_transdc_His_kinase_PgtB.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PIRSF; PIRSF037119; STHK_PgtB; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell inner membrane; Cell membrane; Kinase; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix; Two-component regulatory system.
FT CHAIN 1..668
FT /note="Phosphoglycerate transport system sensor protein
FT PgtB"
FT /id="PRO_0000074836"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 364..416
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 454..663
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 457
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT CONFLICT 151..155
FT /note="IDWLH -> LTGSS (in Ref. 1; AAA68215)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="R -> E (in Ref. 1; AAA68215)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="T -> R (in Ref. 1; AAA68215)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="T -> Y (in Ref. 1; AAA68215)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="L -> A (in Ref. 1; AAA68215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 668 AA; 75403 MW; 4D2C230149412125 CRC64;
MKGRLLQRLR QLSISNSLRG AFLTGALLTL IVSMVSLYSW HEQSSQVRYS LDEYFPRIHS
AFLIEGNLNL AVDQLNEFLL APNTTVRLQL RTQIIQHLDK IERLSQGLQL AERRQLAVIL
QDSRTLLAEL DNALYNMFLV REKVSELSAR IDWLHDDFTT ELNSLVQDFT WQQGTLLDQI
EANQGDAAQY LQRSREVQNE QQQVYTLARI ENQIVDDLRD RLNELKSGNN DGMLVETHIR
YLENLKKTAD ENIRALDDWP STITLRQTID ELLEIGMVKN KMPDTMRDYV AAQKALLDAS
RAREATLGRF RTLLEAQLGS SHQQMQTFNQ RLEQIVRVSG GLILVATLLA LLLAWGLNHY
FIRSRLVKRF TALNQAVVQI GLGRTDSTIP VYGRDELGRI ARLLRHTLGQ LNMQRRQLEQ
EVAERKEIEA DLRAMQDELI QTAKLAVVGQ TMTTLAHEIN QPLNALSMYL FTAGRAIEQG
QSGQARNTLT KAEGLINRID AIIRSLRQFT RRAELETPLY PVDLRQTFVA AWELLAMRHQ
SRQGALSLPT DTVWVSGDEV RIQQVLVNVL ANALDACSHD AVIAVTWQTQ GEALEVYIAD
NGPGWPVALL PSLLKPFTTS KAVGLGIGLS ISVSLMAQMK GDLRLASTLT RNACVVLQFS
VTDVDDVE
