ID SIXA_ECOLI Reviewed; 161 AA.
AC P76502; P77784;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 24-JAN-2024, entry version 163.
DE RecName: Full=Phosphohistidine phosphatase SixA;
DE EC=3.1.3.-;
DE AltName: Full=RX6;
GN Name=sixA; Synonyms=yfcW; OrderedLocusNames=b2340, JW2337;
OS Escherichia coli (strain K12).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=9489669; DOI=10.1046/j.1365-2958.1998.00703.x;
RA Ogino H., Matsubara M., Kato N., Nakamura Y., Mizuno T.;
RT "An Escherichia coli protein that exhibits phosphohistidine phosphatase
RT activity towards the HPt domain of the ArcB sensor involved in the
RT multistep His-Asp phosphorelay.";
RL Mol. Microbiol. 27:573-585(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 80.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
CC -!- FUNCTION: Exhibits phosphohistidine phosphatase activity towards the
CC HPt domain of the ArcB sensor involved in the multistep His-Asp
CC phosphorelay.
CC -!- INTERACTION:
CC P76502; Q2EES9: torI; NbExp=3; IntAct=EBI-548621, EBI-9154838;
CC -!- SIMILARITY: Belongs to the SixA phosphatase family. {ECO:0000305}.
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DR EMBL; D86298; BAA24878.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75400.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16194.2; -; Genomic_DNA.
DR PIR; B65007; B65007.
DR RefSeq; NP_416842.1; NC_000913.3.
DR RefSeq; WP_001195819.1; NZ_STEB01000008.1.
DR PDB; 1UJB; X-ray; 2.06 A; A=1-161.
DR PDB; 1UJC; X-ray; 1.90 A; A=1-161.
DR PDBsum; 1UJB; -.
DR PDBsum; 1UJC; -.
DR AlphaFoldDB; P76502; -.
DR SMR; P76502; -.
DR BioGRID; 4260532; 16.
DR BioGRID; 851156; 8.
DR DIP; DIP-10885N; -.
DR IntAct; P76502; 10.
DR STRING; 511145.b2340; -.
DR jPOST; P76502; -.
DR PaxDb; 511145-b2340; -.
DR EnsemblBacteria; AAC75400; AAC75400; b2340.
DR GeneID; 75202578; -.
DR GeneID; 946815; -.
DR KEGG; ecj:JW2337; -.
DR KEGG; eco:b2340; -.
DR PATRIC; fig|1411691.4.peg.4392; -.
DR EchoBASE; EB3878; -.
DR eggNOG; COG2062; Bacteria.
DR HOGENOM; CLU_084603_1_1_6; -.
DR InParanoid; P76502; -.
DR OMA; MQVLIMR; -.
DR OrthoDB; 92610at2; -.
DR PhylomeDB; P76502; -.
DR BioCyc; EcoCyc:G7211-MONOMER; -.
DR BRENDA; 3.9.1.3; 2026.
DR EvolutionaryTrace; P76502; -.
DR PRO; PR:P76502; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0101006; F:protein histidine phosphatase activity; IDA:EcoliWiki.
DR GO; GO:0036211; P:protein modification process; IMP:EcoliWiki.
DR GO; GO:0070297; P:regulation of phosphorelay signal transduction system; IMP:EcoCyc.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR004449; SixA.
DR NCBIfam; TIGR00249; sixA; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..161
FT /note="Phosphohistidine phosphatase SixA"
FT /id="PRO_0000214568"
FT CONFLICT 80
FT /note="T -> K (in Ref. 2)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1UJC"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:1UJC"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:1UJC"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:1UJC"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1UJC"
FT HELIX 54..66
FT /evidence="ECO:0007829|PDB:1UJC"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1UJC"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:1UJC"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:1UJC"
FT HELIX 111..119
FT /evidence="ECO:0007829|PDB:1UJC"
FT STRAND 133..138
FT /evidence="ECO:0007829|PDB:1UJC"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1UJC"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1UJC"
SQ SEQUENCE 161 AA; 17208 MW; 98D9470A4EBAAA57 CRC64;
MQVFIMRHGD AALDAASDSV RPLTTNGCDE SRLMANWLKG QKVEIERVLV SPFLRAEQTL
EEVGDCLNLP SSAEVLPELT PCGDVGLVSA YLQALTNEGV ASVLVISHLP LVGYLVAELC
PGETPPMFTT SAIASVTLDE SGNGTFNWQM SPCNLKMAKA I
//
