UHPB_SALTY
ID UHPB_SALTY Reviewed; 500 AA.
AC P27668;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Signal transduction histidine-protein kinase/phosphatase UhpB {ECO:0000250|UniProtKB:P09835};
DE EC=2.7.13.3 {ECO:0000250|UniProtKB:P09835};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:P09835};
GN Name=uhpB; OrderedLocusNames=STM3789;
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=1569007; DOI=10.1128/jb.174.9.2754-2762.1992;
RA Island M.D., Wei B.-Y., Kadner R.J.;
RT "Structure and function of the uhp genes for the sugar phosphate transport
RT system in Escherichia coli and Salmonella typhimurium.";
RL J. Bacteriol. 174:2754-2762(1992).
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).
CC -!- FUNCTION: Part of the UhpABC signaling cascade that controls the
CC expression of the hexose phosphate transporter UhpT. UhpB functions as
CC a membrane-associated protein kinase that autophosphorylates in
CC response to interaction with UhpC, and subsequently transfers its
CC phosphate group to the response regulator UhpA. Can also
CC dephosphorylate UhpA. {ECO:0000250|UniProtKB:P09835}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000250|UniProtKB:P09835};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P09835}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:P09835}.
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DR EMBL; M89480; AAA27244.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22647.1; -; Genomic_DNA.
DR PIR; B41853; B41853.
DR RefSeq; NP_462688.1; NC_003197.2.
DR RefSeq; WP_001091264.1; NC_003197.2.
DR AlphaFoldDB; P27668; -.
DR SMR; P27668; -.
DR STRING; 99287.STM3789; -.
DR PaxDb; P27668; -.
DR EnsemblBacteria; AAL22647; AAL22647; STM3789.
DR GeneID; 1255313; -.
DR KEGG; stm:STM3789; -.
DR PATRIC; fig|99287.12.peg.4009; -.
DR HOGENOM; CLU_041023_0_0_6; -.
DR OMA; FCLWVIA; -.
DR PhylomeDB; P27668; -.
DR BioCyc; SENT99287:STM3789-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:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR007895; MASE1.
DR InterPro; IPR011712; Sig_transdc_His_kin_sub3_dim/P.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07730; HisKA_3; 1.
DR Pfam; PF05231; MASE1; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Hydrolase; Kinase;
KW Membrane; Nucleotide-binding; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..500
FT /note="Signal transduction histidine-protein
FT kinase/phosphatase UhpB"
FT /id="PRO_0000074891"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 253..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..500
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P09835"
FT DOMAIN 311..499
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 313
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P09835"
FT CONFLICT 77
FT /note="E -> K (in Ref. 1; AAA27244)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..350
FT /note="QL -> HV (in Ref. 1; AAA27244)"
FT /evidence="ECO:0000305"
FT CONFLICT 383
FT /note="L -> V (in Ref. 1; AAA27244)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 55891 MW; E8DD18724CFE49B8 CRC64;
MNTFFSRLIT VVACFFIFSA AWFCLWSISL HLVERPELAA LLFPFGLRLG LMLQCPRGYW
PVLLGAEWLL VYWLAQEVAL AHLPLLMIGS VLTLLPVALT SRYRHQRDWR TLLLQGAALT
AAALLQSLPW LGQGEEAWNA LLLTLTGGLT LAPICLVFWH YLTSTTWLPL GPSLVSQPVN
WRGRHLIWYL LLFIVSLWLQ LGLPAELSRF TPFCLALPII ALAWHYGWQG ALIATLMNAI
ALIASQTWHD HPVDLLLSLL AQSLTGLLLG AGIQRLRELN QSLQKELARN HRLAERLLET
EESVRRDVAR ELHDDIGQTI TAIRTQAGIV QRLAADNGGV KQSGQLIEQL SLGVYDAVRR
LLGRLRPRQL DDLTLAQAIR SLLREMELES RGIVSHLDWR IDETALSESQ RVTLFRVCQE
GLNNIVKHAN ASAVTLQGWQ QDERLMLVIE DDGSGLPPGS HQQGFGLTGM RERVSALGGT
LTISCTHGTR VSVSLPQRYV
