ID A0A0F7K395_9GAMM Unreviewed; 543 AA.
AC A0A0F7K395;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AAY24_16525 {ECO:0000313|EMBL:AKH21685.1};
OS Sedimenticola thiotaurini.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Sedimenticola.
OX NCBI_TaxID=1543721 {ECO:0000313|EMBL:AKH21685.1, ECO:0000313|Proteomes:UP000034410};
RN [1] {ECO:0000313|EMBL:AKH21685.1, ECO:0000313|Proteomes:UP000034410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIP-G1 {ECO:0000313|EMBL:AKH21685.1,
RC ECO:0000313|Proteomes:UP000034410};
RX PubMed=26089430;
RA Flood B.E., Jones D.S., Bailey J.V.;
RT "Complete Genome Sequence of Sedimenticola thiotaurini Strain SIP-G1, a
RT Polyphosphate- and Polyhydroxyalkanoate-Accumulating Sulfur-Oxidizing
RT Gammaproteobacterium Isolated from Salt Marsh Sediments.";
RL Genome Announc. 3:e00671-15(2015).
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; CP011412; AKH21685.1; -; Genomic_DNA.
DR RefSeq; WP_046860606.1; NZ_CP011412.1.
DR AlphaFoldDB; A0A0F7K395; -.
DR KEGG; seds:AAY24_16525; -.
DR Proteomes; UP000034410; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR014285; N_fixation_neg-reg_NifL.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR02938; nifL_nitrog; 1.
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; PF00989; PAS; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000034410}.
FT DOMAIN 46..92
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 117..171
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 328..539
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 543 AA; 60383 MW; 922E4D601252A32F CRC64;
MIQQKFSAAN GDVIDAISRF LAAPPEGTPA EVIEAFDSFG RGQFLPPKLF LETVEQAPVA
ISITDPAARI LYVNQAFESL TGYHRDEVIG HNESMLSSRS TPIRIYQELW ETIQARQVWQ
GTLVNHKKNK EEYLAELVIS PVLTAKGEIG YYLGMHRDIT AVHQLGQQLK FQTSLTEAAL
DAAPMVMAMI TADRKVLMDN HAYKALLGDC RGVEPVELFL AALEQQIGFD LADACRTGKG
FTNVEVRLDL AGRATPRWFA CSAVRVDELD EAAQNYFREQ QQTRYCLLLI ANEVTASRKR
INEVRLNMIR ASMAEQQMVE TMREAISGAM FKMQVPFNII RAALAMPGNG SDRCNVCQVL
NQALESGDEA MESLQAALPN RAREQTSTVN INEILHEVMR LSTDRLLASG VVVDWRPAAV
LSRVTGRPNA LRGLFKYLID NAIQAVNESG QDYREIRLKS WQDEQELVVE VTDNGPGIPD
AKRLKVFEPF FCGWARADEH AGMGLTMAQE VIVGHGGNME IDAGFRGGCR VLVRLPVKVA
EER
//