ID K9WGV9_9CYAN Unreviewed; 1857 AA.
AC K9WGV9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Mic7113_3277 {ECO:0000313|EMBL:AFZ19014.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ19014.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ19014.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ19014.1,
RC ECO:0000313|Proteomes:UP000010471};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-2012) 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; CP003630; AFZ19014.1; -; Genomic_DNA.
DR RefSeq; WP_015183158.1; NC_019738.1.
DR STRING; 1173027.Mic7113_3277; -.
DR KEGG; mic:Mic7113_3277; -.
DR PATRIC; fig|1173027.3.peg.3610; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG3437; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_236734_0_0_3; -.
DR OrthoDB; 5555607at2; -.
DR Proteomes; UP000010471; 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; 6.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 10.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; 8.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 6.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF13188; PAS_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 7.
DR SMART; SM00091; PAS; 9.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 10.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 7.
DR PROSITE; PS50112; PAS; 6.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010471}.
FT DOMAIN 6..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 374..426
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 427..497
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 500..552
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 560..629
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 687..757
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 760..812
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 947..1017
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1020..1072
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1147..1199
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1200..1271
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1276..1329
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1337..1407
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1410..1462
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1487..1704
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1726..1843
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 267..294
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 543..570
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1453..1483
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1775
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1857 AA; 210275 MW; 17FB56B3FD53A346 CRC64;
MLTHRTVLVI ADSAESDRVY EHQLQQDSNV AYKILTEQYD TPILALSQSQ QIDGILLELH
FPHSNSIQLL RQLKEQMGDR CPPIVVIDSD DAEVAVRAFK NGAADYLVKD RMTPDDLRLS
MHSAIENAEL RRELERSQEQ FQTSVENMLD CFGIFSAMRD ESGQIVDFRI DYLNGAACEN
NRMPKAMQIG RGLCEVLPAH RESGLFDEYC RLVETAEPLI EDSLIYDDTY GKQHLVRAFD
IRATKLNDGF VASWRDVTDR KRLELELSHT VTDLQRHEAA IQQLNRDLTN RVAELQSLLD
IIPVGIAIAT DPSCTQMQNN AYLRQLLGVD PGSNISKSAP VDEQPPYRVF QDGREVPAED
LPMQVAVRLG IDVRDAEFDI LLPNGTVHQL LSYATPLRDD QNQIRGVIGA FLDITERNQD
AAALKASQQR YRELAEAMPQ MVWTADATGA VNYCNQRWYE YTGLNEAESM GLAAANTVHP
DERDRSLTQW SEAIANGQSF EVEYRLCHWG GEYQWFICRA IPTRDSQNQL TGWIGTITNI
DDIKRSEALV QQSEQQLQRQ LAEIEAIYQS APIGLNVLDT ELRFVRINQR LADINGLPIE
AHLGRTVREL FPNLADTLEQ LLHPILKTGE PLLNVEIQGE IPAQPGIKRT WLEHFLPLKA
GERVVGISTV CEEITERIEV EAALRQSEER FRHMADNAPV MIWVTDATGY CTYLNQGWYD
FTGQTEATGL GFGWLDAVHP EDSESSKNVF LSATHRQEAF RLEYRLRRKD GKYRSCLDAA
SPWLGEDGEF KGYIGSVIDI SDVYDELRLR KQAEEALRVS EERYRTLFEN MNEGFCVAEV
LFDEHNKPID YRLLEINSVF EKHSGLKNAQ GKTARELHPE LEQYWIDLYG NVVLTGEPVR
YENYSEALNR WFDVSSFRIG PPGSRKVAIL FEDISKRKQT ERELQESEMR FRTLADNISQ
FAWMADENGQ IFWYSKRWFD YTGTTLEEME GWGWQKVHHP NHVDRVVEKI SRCFETGETW
EDTFPLRGKD GQYRWFLSRA IPVRDEQGKV LRWFGTNTDI TERKQTEAAL QASEERYRSL
IEATAQIIWN EQGDRGEFTT PQPAWSAFTG QTYDELKGWG WLNAVHPDDR AMTTQAWLIA
LENRALYEVE HRVRRHDGVY RHMSVRAVPV FEENGSIREW IGVHTDVTDR KQAEAALHQS
EDRLRMAIES AQLGTWDWNL ITNKLTWDTG CKAMFGLPPD AESSIEVFFE GLHPDDRERL
EQVMQWSFNP ASGGNCDTEY RTIGIQDGIE RWIAAKGQAY FNAAGNPIRF IGTVMDITET
KRREAERKQA EEARRESEIR FGTLASHAPV GIFMTDPQGN CLYVNERWCE MAGMSLEAAQ
ATGWVSALHP DDRERVADLW YQAAQNKQVF AAEYRFQTPQ GKVTWIQGSA TALQRGTGEV
TGYLGTLTDI TERKQVEAER EQLFQQEQAA REAAERANRI KDEFLAVLSH ELRSPLNPIL
GWTKLLQMRK FDETKTAEAL ATIERNAKVQ TQLIDDLLDV AKILRGKLSL NVNSVNLSSA
IAAAIDTVRT AAVAKSISLH PVLPNIGQVS GDAARLQQIV WNLLSNAIKF TPKGGRVDIQ
LNRVGNQAEI AVRDTGRGIN PDFLPHIFES FRQEDASITR QYGGLGLGLA IVRQLVEAHG
GTITADSPGE GLGAAFTVRL PLLDVAPEIQ QTDELPQDKL DITGIRVLAV DDDPDARELL
TVLLTQYGAD VLTVASAVEV LEHLPSFQPD VLVSDIGMPE VDGYTLIQQV RALPSKGGQI
PAIALTAYAR EDDRDRAITS GFQRHVTKPL EPEQLVQAVL ALTRSELNHS LNQNYSV
//
