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Database: UniProt
Entry: Q7M857_WOLSU
LinkDB: Q7M857_WOLSU
Original site: Q7M857_WOLSU 
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
//
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