ID X2H9W7_9NEIS Unreviewed; 606 AA.
AC X2H9W7;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SALWKB2_1753 {ECO:0000313|EMBL:AHN29135.1};
OS Snodgrassella alvi wkB2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Snodgrassella.
OX NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN29135.1, ECO:0000313|Proteomes:UP000019668};
RN [1] {ECO:0000313|EMBL:AHN29135.1, ECO:0000313|Proteomes:UP000019668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WkB2 {ECO:0000313|EMBL:AHN29135.1};
RX PubMed=25053814;
RA Kwong W.K., Engel P., Koch H., Moran N.A.;
RT "Genomics and host specialization of honey bee and bumble bee gut
RT symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014).
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; CP007446; AHN29135.1; -; Genomic_DNA.
DR RefSeq; WP_025331314.1; NZ_CP091515.1.
DR AlphaFoldDB; X2H9W7; -.
DR STRING; 1196094.SALWKB2_1753; -.
DR GeneID; 32536420; -.
DR KEGG; salv:SALWKB2_1753; -.
DR PATRIC; fig|1196094.4.peg.1754; -.
DR HOGENOM; CLU_000445_89_29_4; -.
DR OrthoDB; 224978at2; -.
DR Proteomes; UP000019668; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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; 1.
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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
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); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AHN29135.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000313|EMBL:AHN29135.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 14..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 263..308
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 398..606
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 606 AA; 67894 MW; A83B82095EF04536 CRC64;
MNTSFLQRLY PERISARIFL LVTFLSCFSI FVCAVLIDKE GRELLRQEKS HKLYAITKTL
DLLLGDAYQQ VDKSLPRTQQ ITQLNQYLSP KIEPLLKDMP NIAAGYYHKQ LDAIVLYAPQ
SAYGVNVGKS IPAEHKGREV MTSGRHMVET GQQVRGNIMN AMIPIVRNNQ IIGYIWANET
LDDIEKQAFV FDKNVIIISL ICMLSCICIA SVLSRKLNTD INIIKQGLEK LPFSLDRRLP
VIRGELNEIV SGINSLAEKL RKTKTINELI LENTLDAVIT VDNNGFITML NPAAEKITGY
QLEQVLGRPY STIVDDKNFQ SPLLDTLYNG IDHVGVEVDF PVARQIIRIS ASTSHLKDYQ
GNIIGAVVIF KDITEREEVE KLIQQTERLV ALGELMAGIA HEIRNPLAAV RGFVQYLQND
LPRAEQNEYL DIILKEVDSI NQVIQQLLDF SVPSKNYYVS VQLNDLINEV LVLVNSSHRS
NNIVLTLSLA SQLPPLYLDK ELIKQAILNL LINAIQAVSD QGNIEISTLM SANQKYQLIR
IKDDGEGIKS EIMDKIFTPF FTTKISGTGL GLAMVEKIVS SHKGQISIKN NEHSNGVTVE
VALPVN
//
