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Database: UniProt
Entry: Q7M884_WOLSU
LinkDB: Q7M884_WOLSU
Original site: Q7M884_WOLSU 
ID   Q7M884_WOLSU            Unreviewed;       409 AA.
AC   Q7M884;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=WS1818 {ECO:0000313|EMBL:CAE10833.1};
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:CAE10833.1, 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; BX571661; CAE10833.1; -; Genomic_DNA.
DR   RefSeq; WP_011139616.1; NC_005090.1.
DR   AlphaFoldDB; Q7M884; -.
DR   STRING; 273121.WS1818; -.
DR   KEGG; wsu:WS1818; -.
DR   eggNOG; COG0642; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_051843_0_0_7; -.
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; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR047994; ArsS-like.
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   NCBIfam; NF038389; ArsS_fam_HK; 1.
DR   PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR   PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAE10833.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000422};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        131..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          155..202
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          210..409
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   409 AA;  46984 MW;  12D5DCE22E0E5EE0 CRC64;
     MTKNSIIVKI TILFAVALLS LSAFSFYFIK MQIDKESSES QRKYGQFIAT INQIMRYGGN
     VELIEKYLAE LEFHIVNDDQ IKENLSKQID PHFKGVIAKI VRDNESIYLL LQTPERVTLY
     RDSFKTVFKN YYLLTFIAFF IVVFLYVLVI KSLLPLKSLR KEIRKFAEGR TDIHCALEQN
     DEIGELANEF DNAVKKIAAL NESRHLFLRT IMHELKTPLT KGRIVAEMID SPKQKERLCS
     VFHRLNGLID EFAKIEEMSS KNYQVSKNEY RLHAILHHVL KKLMIESEQA PTLLDLPAQE
     VIVKADFELL SLAIKNLLDN ALKYSHGGKV FLEARGDSLN VKNFGAPLPY PIEEYFKPFF
     KDAKNPHSQG LGLGLYIAKS TLEAQGLPLL YQYEEGVHQF TLKGVVVEK
//
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