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Database: UniProt
Entry: C6SGR7_NEIME
LinkDB: C6SGR7_NEIME
Original site: C6SGR7_NEIME 
ID   C6SGR7_NEIME            Unreviewed;       468 AA.
AC   C6SGR7;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NMW_0133 {ECO:0000313|EMBL:CBA04246.1};
OS   Neisseria meningitidis alpha275.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=295996 {ECO:0000313|EMBL:CBA04246.1};
RN   [1] {ECO:0000313|EMBL:CBA04246.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Alpha275 {ECO:0000313|EMBL:CBA04246.1};
RX   PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA   Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA   Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA   Linke B., Vogel U., Frosch M.;
RT   "Whole-genome comparison of disease and carriage strains provides insights
RT   into virulence evolution in Neisseria meningitidis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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; AM889138; CBA04246.1; -; Genomic_DNA.
DR   AlphaFoldDB; C6SGR7; -.
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; cd16949; HATPase_CpxA-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR   PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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:CBA04246.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBA04246.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          180..235
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          243..458
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   468 AA;  52782 MW;  A2DE9A0A587628B2 CRC64;
     MKLFQRIFAT FCAVIVCAIF VASFSFWLVQ NTLAENQFNQ RRTIETTLMG SIISAFRARG
     DAGAREILTE WKDSPVSSGV YVIQGDEKKD ILNRYIDSYT IERARLFAAG HPHSNLVHIE
     YDRFGEEYLF FTKDWDKLQA RRLPSPLLIP GLPLAPIWHE LIILSFIIIV GLLMAYILAG
     NIAKPIRILG NGMDRVANGE LETRISQQVD DRDDELSHLA IQFDKMVEKL EKLVAKERHL
     LHHVSHEMRS PLARMQAIVG LIQAQPQKQE QYLKRLEGEL TRMDTLAGEL LTLSRLETSN
     MALEKESLKL LPFLGNLVED NQSIAQKNGQ TVTLSADGKI PENTTILANE SYLYRAFDNV
     IRNAVNYSPE GSTILINIGQ DHKHWIIDVT DNGPGVDEMQ LPHIFTAFYR ADSSANKPGT
     GLGLALTQHI IEQHCGKIIA ENIKPNGLRM RFILPKKKTG SKTEKSAN
//
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