ID A0A248JTH2_9PROT Unreviewed; 604 AA.
AC A0A248JTH2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Y958_13235 {ECO:0000313|EMBL:ASG22017.1};
OS Nitrospirillum amazonense CBAmc.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1441467 {ECO:0000313|EMBL:ASG22017.1, ECO:0000313|Proteomes:UP000197153};
RN [1] {ECO:0000313|EMBL:ASG22017.1, ECO:0000313|Proteomes:UP000197153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBAmC {ECO:0000313|EMBL:ASG22017.1,
RC ECO:0000313|Proteomes:UP000197153};
RA Schwab S., dos Santos Teixeira K.R., Simoes Araujo J.L., Soares Vidal M.,
RA Borges de Freitas H.R., Rivello Crivelaro A.L., Bueno de Camargo Nunes A.,
RA dos Santos C.M., Palmeira da Silva Rosa D., da Silva Padilha D.,
RA da Silva E., Araujo Terra L., Soares Mendes V., Farinelli L.,
RA Magalhaes Cruz L., Baldani J.I.;
RT "Complete genome sequence of Nitrospirillum amazonense strain CBAmC, an
RT endophytic nitrogen-fixing and plant growth-promoting bacterium, isolated
RT from sugarcane.";
RL Submitted (JUN-2017) 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};
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DR EMBL; CP022110; ASG22017.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A248JTH2; -.
DR KEGG; nao:Y958_13235; -.
DR Proteomes; UP000197153; Chromosome 1.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 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 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; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12860; PAS_7; 2.
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; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ASG22017.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000197153};
KW Transferase {ECO:0000313|EMBL:ASG22017.1}.
FT DOMAIN 378..598
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 604 AA; 66100 MW; 46E8CDDE3236C6BD CRC64;
MRRADGALVW CNQAYGTAVG MPPEEVVAQG VELVTGPGAG QLLAARALSG REPASESRHV
IVAGQRQLLR LTETPLGIPL EGGAALLGHA LDTTREQELS SELERHIAAH ADVLEHLGSA
IAIYGADSKL KFHNRSYARL WGLDESWLET EPSYGEVLED LRSRRRLQEE VDFPRWKRAQ
LALFTNLTEP REDLVHLPDG TTLRTIAVPH PFGGLMFVLE DVTNALALES SYNTLMAVQQ
ETLDNLAEGV AVFGGDGRLK LWNPSFARIW RLKGPDLNGE PHITQVIDKL QPLLDHDGDW
PARRRTMIAD LLERSSYAGR LERTDRSIVD VSNVPLPDGA VLISVLDITD SVRVEEALRA
SNEALATADR LKSEFIANVS YQLRTPLNAI MGFAEILNNQ YFGALNERQA DYTKGVLEAS
RRLLALINDI LDLATIEAGF MTLDRSPVDV GQLLEAVSGL TLDWARKQDV TLLVQVPPDI
GNLDADERRL KQALYNLVSN AVKFTPPGGQ VTLSAKRQMG EGGPEMVLSV SDTGIGIPAA
DRQRVFNKFE RGEVQNHPAG AGLGLSLVKS FVELHGGHVE ISDSDQGTLI QCHLPLRQNA
VMAV
//