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Database: UniProt
Entry: F4H9X4_GALAU
LinkDB: F4H9X4_GALAU
Original site: F4H9X4_GALAU 
ID   F4H9X4_GALAU            Unreviewed;       567 AA.
AC   F4H9X4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=UMN179_01263 {ECO:0000313|EMBL:AEC17282.1};
OS   Gallibacterium anatis (strain UMN179) (Pasteurella anatis).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Gallibacterium.
OX   NCBI_TaxID=1005058 {ECO:0000313|EMBL:AEC17282.1, ECO:0000313|Proteomes:UP000006908};
RN   [1] {ECO:0000313|EMBL:AEC17282.1, ECO:0000313|Proteomes:UP000006908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN179 {ECO:0000313|EMBL:AEC17282.1,
RC   ECO:0000313|Proteomes:UP000006908};
RX   PubMed=21602325; DOI=10.1128/JB.05177-11;
RA   Johnson T.J., Fernandez-Alarcon C., Bojesen A.M., Nolan L.K., Trampel D.W.,
RA   Seemann T.;
RT   "Complete genome sequence of Gallibacterium anatis strain UMN179, isolated
RT   from a laying hen with peritonitis.";
RL   J. Bacteriol. 193:3676-3677(2011).
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; CP002667; AEC17282.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4H9X4; -.
DR   STRING; 1005058.UMN179_01263; -.
DR   KEGG; gan:UMN179_01263; -.
DR   eggNOG; COG3221; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_011260_3_0_6; -.
DR   Proteomes; UP000006908; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
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   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 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; IPR004358; Sig_transdc_His_kin-like_C.
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; PF12974; Phosphonate-bd; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:AEC17282.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000313|EMBL:AEC17282.1}.
FT   DOMAIN          353..561
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   567 AA;  64960 MW;  3F3F92E7AA86C968 CRC64;
     MLSLTYIMLS LFPFFAGADN WKIGILAQRG ETFLSQQWQP WINWLNQRDP QQHFSLVPLQ
     LDDLSQDKAD NIDFILTNQS QFFYLNDQPV RWLATLQSPR QQHTNAGKVG SAILVNTESN
     FHQIADLKGK TLSAVGENAF GGFLLGYNVL YQQGLVEGKN IFFRFSGFPV DNTVFWLQQH
     KVDAAIVPVC ILEDLAREGK VNFSDFRVLA PQSNDLGCVS STPLLPNWSL AAMAQVPDNI
     VKKIMTILLG DVPADLPQWN PPYSDQQADN ILRNLFRHPQ QQNLWQSVKY WINQHQWQLL
     LLLFFIIFNY LWISYQVHRK SKALTQAHQE MRLYEQQLIK ADRLSILGEM SAGIAHEINQ
     PLTAIGMYSE GLKQQLKQRS DATFELQILD KIQVQVDRSR QIMRNLTGWA KGKEDEKLHN
     IELKSCLEKT IDFIRQHYNS RAKIRLICAK QWQVCIKKTM LEQILCNCLL NALQAQANKI
     VISVQEKENS IQILIVDNGK GFSETELAFP FVPFRSRKKE GLGLGLTLCQ RLIHSMRGEI
     YLKNRPADKG AMVILELPLN QGVGSKQ
//
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