ID A0A060NI32_9BURK Unreviewed; 727 AA.
AC A0A060NI32;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SRAA_1033 {ECO:0000313|EMBL:BAO80887.1};
OS Serpentinimonas raichei.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Serpentinimonas.
OX NCBI_TaxID=1458425 {ECO:0000313|EMBL:BAO80887.1, ECO:0000313|Proteomes:UP000067461};
RN [1] {ECO:0000313|EMBL:BAO80887.1, ECO:0000313|Proteomes:UP000067461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1 {ECO:0000313|EMBL:BAO80887.1,
RC ECO:0000313|Proteomes:UP000067461};
RX PubMed=24845058; DOI=10.1038/ncomms4900;
RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA Nealson K.H.;
RT "Physiological and genomic features of highly alkaliphilic hydrogen-
RT utilizing Betaproteobacteria from a continental serpentinizing site.";
RL Nat. Commun. 5:3900-3900(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; AP014568; BAO80887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A060NI32; -.
DR STRING; 1458425.SRAA_1033; -.
DR KEGG; cbaa:SRAA_1033; -.
DR HOGENOM; CLU_011260_1_0_4; -.
DR OrthoDB; 9812260at2; -.
DR Proteomes; UP000067461; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16921; HATPase_FilI-like; 1.
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 Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 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 SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:BAO80887.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000067461};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:BAO80887.1}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..727
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001588897"
FT DOMAIN 501..717
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 727 AA; 81570 MW; 32E67255F0650111 CRC64;
MRRLLYLCLL CLLPLLAGAS ATGTAPAPGA ASATERFVLG VLATRPLPLV EQEHQPLADY
LAQQLNAEVQ LHVLDDAALN RALERGQIDF LLTSPGHYMI VRRQFPLAGL LATLIRQDNG
QQTTQLGGVI IALAARTDLR TLADLEGQRI AALPPRTLAG YQIQAYELLQ AGFDVQRDFA
FTHFEHHDAV VQAVLTGQAD AGFVRTGILE ALKLEGRLRA QQLHVIHAQQ HPGFPFLVST
RLYPEWAFAA MERVDPLVAR RAAAALMLLP PGHPVTQGTQ IAGFAPPQVY IEVEDVTRAL
RLPPFDAAPE FTWADVWERH KNPLLALAVS FLAIVALLGF SLWHRRELQR QRDALDRLIQ
LWPQPMLLIH QQRFVQSNRA ALALLGLEHE HELLGRTPWD ISPPQQSDGL DSRQRVQAVL
DAVQHGQVTR LDWDLSQRDG ALVAVEFTLL ALEPHAAQRS NQRILCGWTD LTLRKQTERL
LQQHADNLAR SNAELEQFAY VASHDLRQPL RMINSYVQLL ERRLADRLDE ETRQMMGFVT
QAAQRMDQML VALLEYSRVG RLGEPMEALS MREVLDEALR FLAPLSAETQ AQIRVRGHWP
ELLISRNEIT RLWQNLVGNS LKFRAPDRAP QIEISAAPDE QGWRFEVADN GIGIDPGQFE
RLFRVFQRLH TRSEFEGTGI GLALARKIVE RHGGRIWVES AGLGQGSRFV FFLPTQSPDS
AHAEPQS
//
