ID H2FZD2_OCESG Unreviewed; 944 AA.
AC H2FZD2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=GU3_02570 {ECO:0000313|EMBL:AEY00271.1};
OS Oceanimonas sp. (strain GK1 / IBRC-M 10197).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanimonas.
OX NCBI_TaxID=511062 {ECO:0000313|EMBL:AEY00271.1, ECO:0000313|Proteomes:UP000007742};
RN [1] {ECO:0000313|EMBL:AEY00271.1, ECO:0000313|Proteomes:UP000007742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GK1 {ECO:0000313|EMBL:AEY00271.1,
RC ECO:0000313|Proteomes:UP000007742};
RX PubMed=22461556; DOI=10.1128/JB.00023-12;
RA Parsa Yeganeh L., Azarbaijani R., Sarikhan S., Mousavi H., Ramezani M.,
RA Amoozegar M.A., Shahzadeh Fazeli A., Salekdeh G.H.;
RT "Complete genome sequence of Oceanimonas sp. GK1, a halotolerant bacterium
RT from Gavkhouni Wetland in Iran.";
RL J. Bacteriol. 194:2123-2124(2012).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003171; AEY00271.1; -; Genomic_DNA.
DR RefSeq; WP_014291007.1; NC_016745.1.
DR AlphaFoldDB; H2FZD2; -.
DR STRING; 511062.GU3_02570; -.
DR KEGG; oce:GU3_02570; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_46_6; -.
DR OrthoDB; 9804645at2; -.
DR Proteomes; UP000007742; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 2.
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; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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; 2.
DR PROSITE; PS50112; PAS; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000007742}.
FT DOMAIN 542..593
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 594..664
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 668..719
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 723..943
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 944 AA; 105618 MW; 46975D9AE4EA6929 CRC64;
MKTPDLPFDE LQRLEALRRT GLLDTPPEAR FDRLTRIAQQ SFGVDIALVS LVDSERQWFK
STQGLDACET RRDISFCGHA ILDSRVFVVE DALQDERFAD NPLVTAAPHI RFYAGAPLHS
IEGFRIGTLC VIDSRPRRFD EQDGELLRNL ADCVEEQLSR QRLDELRKSL AESEYRARLI
IEGANIGTWQ CDMQTGQCRF NDRWAEMLGW RLDELGDTNI DTWKSRVHSE DLAPAEAMLE
RHIQGLEPVY ECRIRMRHKD GHWVWVHSRG RLLDCGADGK PGIIYGTHID TSAEQEALAQ
LERRNRALAM LNRMAFKLTG SVDERITQAL ALGREFLQLD VAIASEIIGD VYVVRWVSVP
GEASIAPGLQ FKVDQTYCRL MLAQDGVMAI NHMGRSEYSD TACYRTMGLE SYIATRLLVD
GELFGTLNFS SAGVRDTPFD DTDRMFLALM ARWLGDQLSR QRQQARLDKL ATQLPGMIYQ
YRRWPDGRSA FPYSSAGIEQ VYRLDAEVVR NNAEAVFERI YPPDLEAVAE SIVRSEQGLS
DWHAQYRVLQ ADGGTHWVEG RARPERLEDG STIWHGYLTD IEHEKQAELA LVVSEQRLRG
LFELSSIGIA LSDAGSGRIL DVNRALLEAS GYGKTELLGL TLPALTPTEH QPHDAVAQAT
LNEAGRYAPF EKELLHRSGA RFPVRQQGML IRDAGGRQLV WTLIEDITEL KKVERMQKEF
VSTVSHELRT PLTAISGALG LLSQGAMGEL APSALRLVAL AHANSQRLNL LINDLLDMEK
LVAGKMQFDV QPLALHELVQ DAVEGHRPLG ESRGVRLTLG AQLDGDRVLA DRDRLFQALA
NLLSNAVKFS PDGGEVRIST ESAGNGRVRL RVQDQGEGVP EAFRGRIFEK FAQADSSDTR
KKGGTGLGLA ITRELMERMN GAVGFESTEG EGACFWLDIL VAKY
//