ID Q7M857_WOLSU Unreviewed; 765 AA.
AC Q7M857;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 24-JAN-2024, entry version 116.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=RHPS {ECO:0000313|EMBL:CAE10872.1};
GN OrderedLocusNames=WS1861 {ECO:0000313|EMBL:CAE10872.1};
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121 {ECO:0000313|Proteomes:UP000000422};
RN [1] {ECO:0000313|EMBL:CAE10872.1, ECO:0000313|Proteomes:UP000000422}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 /
RC NCTC 11488 / FDC 602W {ECO:0000313|Proteomes:UP000000422};
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon JM., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR EMBL; BX571662; CAE10872.1; -; Genomic_DNA.
DR RefSeq; WP_011139655.1; NC_005090.1.
DR AlphaFoldDB; Q7M857; -.
DR STRING; 273121.WS1861; -.
DR KEGG; wsu:WS1861; -.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_364815_0_0_7; -.
DR OMA; VIFENIT; -.
DR Proteomes; UP000000422; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
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; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF42; TWO-COMPONENT SENSOR PPRA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:CAE10872.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000000422};
KW Transferase {ECO:0000313|EMBL:CAE10872.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..228
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 242..312
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 315..367
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 393..437
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 540..760
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 765 AA; 87497 MW; DD79908C3C9A7C83 CRC64;
MFVTFYLSIV LFLLSLLLAS FTLKREIDTK KASSPLQKKL IVAGVFIACA LGFGVYGVYD
YHQTLTQERQ RGFERLQGIE HLFRNELSRA DISIFDTDNP RRHDLLGRLA LYVSNSADVS
YACLVNQKHP IGAYLLDRKS NYAKPLQECS SLELERTPKG FGALLLGELY APWRFDSIIE
NRFDRIEARF FLDTRRLEGA VYDSFNSVGN LILGVSILIF VFSFVLALRK ERFEESVLGY
SQGRAFDKII ESIPMPILYK NMEGSYLGCN SKFLELSGKS REEVIGFRVG DLLDKKSAME
IEECERHLKE KGECPSHDIR FVDHRGEECF IRVYKTLLTN NFDEPVGILG FFVDMSEYHQ
SQRELKERQE QLEFFSEQLE KQMEYEISGR LNSERRYKQL FDSGRDGIFV VQMDEEEGVA
QIVEANWSAH EMFGYSQGAF EELAFASLVD KGEREGVERL LKELPLKGGA LIESHFVLLE
HRSIPIELSI QSFLLEEKRT LYVSARDITE RLRLEEEKRV QENLLVQQSK MASMGEMIGA
IAHQWKQPLN AIYLMCQGLK ESFAYNELDE AEMDRFVSGA MKQVEFMSRT ITDFRNFFMP
SKEKCAFALK EALLEMHSIL APQFSKHDIE VRITQEGEGS VVAYGYPNEF KQVALNLMNN
SRDAIEERIR CGEKISGKIE VRISSEGDYA CARIKDNGGG IPDEILKNIF EPYFSTKGEK
GTGIGLSIAK MIIEKNMNGK IRAYNEEKGA VFEIRLPLSG ARSNA
//