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Database: UniProt
Entry: G9ZXV7_9PROT
LinkDB: G9ZXV7_9PROT
Original site: G9ZXV7_9PROT 
ID   G9ZXV7_9PROT            Unreviewed;       833 AA.
AC   G9ZXV7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, 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   ORFNames=HMPREF9946_01389 {ECO:0000313|EMBL:EHM02195.1};
OS   Acetobacteraceae bacterium AT-5844.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=1054213 {ECO:0000313|EMBL:EHM02195.1, ECO:0000313|Proteomes:UP000003292};
RN   [1] {ECO:0000313|EMBL:EHM02195.1, ECO:0000313|Proteomes:UP000003292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AT-5844 {ECO:0000313|Proteomes:UP000003292};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHM02195.1}.
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DR   EMBL; AGEZ01000045; EHM02195.1; -; Genomic_DNA.
DR   AlphaFoldDB; G9ZXV7; -.
DR   STRING; 1054213.HMPREF9946_01389; -.
DR   PATRIC; fig|1054213.3.peg.1282; -.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG3920; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_44_5; -.
DR   OrthoDB; 9795133at2; -.
DR   Proteomes; UP000003292; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 6.10.250.2580; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF08448; PAS_4; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003292}.
FT   DOMAIN          195..265
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          268..321
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          315..354
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          393..445
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          521..574
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          601..827
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   833 AA;  91001 MW;  8A1BB68524A8794D CRC64;
     MLSWADAHGR WRDGSGRAGA GDGPKSCLAA LRAAGLFGAP PEERFDRLTR LARRLVRAPV
     ALVTLLDDDR QFFLSAQGLP EPLAQLRETP LSYSFCRTVV ETGLPLAVAD AREDPCLREN
     PAIEELGVVA YLAMPLALPD GCVVGALCVI DWAPRQWSEE DRQALADLAG AVMTELAMSL
     RLRDLDAANA ALRESEARHR ALFEVSPQVV WFADAAGRLT YVNQHYAALV GLPAEQALGE
     GWLTSIHPED HESVRAAWAE AVGRADGYEV EFRIRRRSDG SYRWHLCRGA PVHDAAGRVE
     RWIGIAIDID DRRRAEQALR GLIEALGVAV YTTDADGRLT FYNEAAAALW GWRPPLGTMH
     WCGSLRLYSP DGVPLRHEEC PMGVALRENR PIRGEEAVAE RPDGTRVPFI AYPTPLRDAA
     GELVGGLNVL VDITKRKAVE AALARSEARL QLALQAGRLA FWELDMATGS VVRGPSHDLI
     YGYETSLPQW SFQAFLRHVI LDDRAKAQRF YEVLTESRTG AFLECRIRRA NDGEVRWVEV
     HGHPHLGADG KVARLLGIVR DVTERKRTEA ALRKNEARLR ELQGELLHVS RLSAAGEMAS
     ALAHELNQPL TATVSAVRAA QRILAAWPGQ PAAQGDIHDA IDLAAEQALR AGQIIRRLRD
     FVGWDGEGER RLEDLAKLAK EAGALALVGA REHGVRVAFR FGPELPSVLV DRIQIQQVLV
     NLMRNAMEAM EAMAAGEGSA SPRRELTVTA AATSGDTVEV AVADTGPGLA LENTERLFDP
     FVSTKPSGMG LGLSICRSII ESHGGRLWTE PNPGGGAVFR FTLPSAPSEI DYR
//
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