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Database: UniProt
Entry: A0A1U7J6I2_9CYAN
LinkDB: A0A1U7J6I2_9CYAN
Original site: A0A1U7J6I2_9CYAN 
ID   A0A1U7J6I2_9CYAN        Unreviewed;       709 AA.
AC   A0A1U7J6I2;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=NIES30_10780 {ECO:0000313|EMBL:OKH48487.1};
OS   Phormidium tenue NIES-30.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Phormidium.
OX   NCBI_TaxID=549789 {ECO:0000313|EMBL:OKH48487.1, ECO:0000313|Proteomes:UP000185557};
RN   [1] {ECO:0000313|EMBL:OKH48487.1, ECO:0000313|Proteomes:UP000185557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-30 {ECO:0000313|EMBL:OKH48487.1,
RC   ECO:0000313|Proteomes:UP000185557};
RA   Zhu T., Hou S., Lu X., Hess W.R.;
RT   "Draft Genome Sequences of Nine Cyanobacterial Strains from Diverse
RT   Habitats.";
RL   Submitted (NOV-2016) 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:OKH48487.1}.
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DR   EMBL; MRCG01000006; OKH48487.1; -; Genomic_DNA.
DR   RefSeq; WP_073608414.1; NZ_MRCG01000006.1.
DR   AlphaFoldDB; A0A1U7J6I2; -.
DR   STRING; 549789.NIES30_10780; -.
DR   OrthoDB; 510512at2; -.
DR   Proteomes; UP000185557; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd16934; HATPase_RsbT-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 2.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:OKH48487.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000185557};
KW   Transferase {ECO:0000313|EMBL:OKH48487.1}.
FT   DOMAIN          222..441
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          463..576
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          583..699
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          157..191
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         512
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         632
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   709 AA;  78102 MW;  1514315CEECFF906 CRC64;
     MTTLFTLEIH YEQDVVQARQ RTRELAEQLG FDGQDQVRLA TAVSEIARNA FQYAQGGTVQ
     FDLAENPQTF LIQVQDQGGG IPHLSDVLDG RYQSSTGMGL GIVGTRRLMD IFEIASSEQG
     TTVSLGKALP KRSPSFTNSQ LEQIRETVVG RSPQNPYDEI QRQNQELLRA MAELRKREEE
     LTYLNRELED TNRGVIALYA ELDEKASSLQ QANELKTRFL SNMSHEFRTP LNSILSLSRM
     LLTRLDGELS LEQEKQVTYI QKAADGLSEL VNDLLDLAKV EAGKTEVNPS SFEVSDLFAT
     LRGMLRPLLV QGSSVSLVFD EPDGLPSLYS DEGKIAQILR NFISNALKFT EQGEVRVSAE
     QVGQMIRLSV SDTGIGIAPA DQERVFEDFV QIESDLQKQV KGTGLGLPIS AKLAELMEGS
     VSVHSELGQG STFSVCIPIV YPKVTELPDS LQPIISLNPA RLPILAIEDH IETLFIYEKH
     LQASRYQLIA TRTLAQARQA LEQLQPAAIV LDILLEGQNG WTFLRELKSD EATRNIPVLV
     ITVVDNEKQA VALGANGFLI KPVDQLTLLT KLNTLVGQGK TQKLLLIDDD PAYQYVVKQL
     LTNLPLQFLE AASGREGLTV AESEQPSAIL LDLEMPGLSG FDALEQLQRN PVTQSIPVII
     YSSTQLSLET RSRLAKQGVA ILSKDKTSQA EAASHLREAL AKAGLVLDA
//
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