ID Q7NPF6_GLOVI Unreviewed; 785 AA.
AC Q7NPF6;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=gll0099 {ECO:0000313|EMBL:BAC88040.1};
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221 {ECO:0000313|EMBL:BAC88040.1, ECO:0000313|Proteomes:UP000000557};
RN [1] {ECO:0000313|EMBL:BAC88040.1, ECO:0000313|Proteomes:UP000000557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421 {ECO:0000313|Proteomes:UP000000557};
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC88040.1; -; Genomic_DNA.
DR RefSeq; NP_923045.1; NC_005125.1.
DR AlphaFoldDB; Q7NPF6; -.
DR STRING; 251221.gene:10757568; -.
DR EnsemblBacteria; BAC88040; BAC88040; BAC88040.
DR KEGG; gvi:gll0099; -.
DR PATRIC; fig|251221.4.peg.101; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_000445_114_15_3; -.
DR InParanoid; Q7NPF6; -.
DR OrthoDB; 9768069at2; -.
DR PhylomeDB; Q7NPF6; -.
DR Proteomes; UP000000557; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IBA:GO_Central.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; IPR011006; CheY-like_superfamily.
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 InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 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.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000557};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 89..159
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 162..214
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 414..632
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 662..780
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 711
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 785 AA; 85183 MW; CB5D8C44EDD06874 CRC64;
MQERRRHVCW MCLVCSADRA LPLERPIHST WPTEVSAADP ADPAASEGLV MACSPENLLA
EIAALREHNA RLEALLGEGR LKAPALLESE ERYRSLITVT SAIVWTAGSD GAIVEEVPSW
EEFTGQSPEQ YQGWGWVEML HPEDRASTAE IWRQANANKR PVEVEYRLRR RDGEYRHMVA
RGVPLLNAGG RLCSWVGTVT DIHDRKVAEQ QRELRLLQAK RHTTRLQKLA EASLAINSAL
SIQQVLQGIT EQAAALIGAH MALTSLTPER DWARAVHTVY LSDKYRYWHH GEARLGGVGI
AADVCRTNRP ARLTQSQLEG HPQGRLLAFG ATDRPALRGW LAAPLVGRDG RNIGLIQLSD
KHEGDFSEED EAIAVQLAQL ASVAIENTRL FEAEQAAKVD AEEANRLKDE FLATLSHELR
SPLTAILGWT KLLRQVDLGA VRAAHALEVI ERNALAQNQL IEDLLDISRI VAGKLRIEAA
AVDLAGVIEA AIGTVRPAAQ ARAIEVDTEI EPGVPLLMGD ATRLQQVVWN LLANAVKFTP
NGGRVRVRLS RRGTAAEVAV SDSGLGIAPH LLPHVFERFR QADSSSTRSH GGLGLGLAIV
RQLVELHSGT VSAASPGEGQ GATFTVRLPF DGARTLLAGD HSPGDWTRES PTACCGRLDG
LRVLVVDDEP QARELVRTTL ELCGAQVATA GSAAEALAEV RRSKPAVLVS DIAMPGEDGY
ALLRQLRLLE AECGGRIPAV ALTAYARVED RRRALLAGFQ THLSKPVEPS ELVAAVANLS
CQAAI
//
