ID K9WQR3_9CYAN Unreviewed; 1153 AA.
AC K9WQR3;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Mic7113_6526 {ECO:0000313|EMBL:AFZ22104.1};
OS Allocoleopsis franciscana PCC 7113.
OG Plasmid pMIC7113.02 {ECO:0000313|EMBL:AFZ22104.1,
OG ECO:0000313|Proteomes:UP000010471}.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ22104.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ22104.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ22104.1,
RC ECO:0000313|Proteomes:UP000010471};
RC PLASMID=pMIC7113.02 {ECO:0000313|EMBL:AFZ22104.1,
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 plasmid 2 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};
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DR EMBL; CP003632; AFZ22104.1; -; Genomic_DNA.
DR RefSeq; WP_015211498.1; NC_019760.1.
DR AlphaFoldDB; K9WQR3; -.
DR KEGG; mic:Mic7113_6526; -.
DR PATRIC; fig|1173027.3.peg.7220; -.
DR HOGENOM; CLU_000650_2_1_3; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000010471; Plasmid pMIC7113.02.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR CDD; cd16916; HATPase_CheA-like; 1.
DR CDD; cd00088; HPT; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004105; CheA-like_dim.
DR InterPro; IPR036061; CheW-like_dom_sf.
DR InterPro; IPR002545; CheW-lke_dom.
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; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43395:SF1; CHEMOTAXIS PROTEIN CHEA; 1.
DR PANTHER; PTHR43395; SENSOR HISTIDINE KINASE CHEA; 1.
DR Pfam; PF01584; CheW; 1.
DR Pfam; PF02895; H-kinase_dim; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00260; CheW; 1.
DR SMART; SM01231; H-kinase_dim; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF50341; CheW-like; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50851; CHEW; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFZ22104.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Plasmid {ECO:0000313|EMBL:AFZ22104.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW Transferase {ECO:0000313|EMBL:AFZ22104.1}.
FT DOMAIN 2..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 559..819
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 821..963
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1022..1139
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 535..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 488..515
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 546..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1072
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1153 AA; 126720 MW; DA723B24F2097585 CRC64;
MSQDKEREIQ LQFLEEAQEY LDTIESVLLG LAGSHIDGQQ MDAVLRAAHS VKGGAGMMGY
QSLSQLAHRL EDSFKVLKAQ RNSIVIDPEL ESLLLVAVDR LRQVLVLNRQ GTDVEQQWMV
NVGTPVFDQL SSRLGDPVAD DAATMLGAED GTNVAALLFE TEVEGCLKRL ESVLDDPQTP
CLEEELSIMA QELGGLGEML QLEAFTQLCE SVIQHLEAAP DAVREIASSA LTAWKRSQAL
VLVGQMNILP TQIDWSRGEM PFDISTDQRT QPISIPTQIE ATDLIYSEEE LAAAFDIDTS
EPTPFFTNIP IPSLTADEAE VEHLMDEIFE GPVVVPFNHT STSASVPIDS PTHEDIAAEH
SLFVEENWQE EELTAAFDID VPTTLPTVPP TPVRSYTTQY VKSKDEYTEE SVAVPTSSTS
LSREVQTVKS EVISRDIKWQ EVKPDSTSSP QTAETQENTV RIPVRQLDRL NELFGELTIE
RNGLSLHLGR LRNLMETLSR RVGNLEQSNM RLRTTYDTVA TQSVLEGTLL RGLGSGNWGH
GGQEKPGNTA FSSKSAQSSS PHETTFPLNS QFDALEMDRY SDLHLLSMEV METIVQIQEV
TSDIGLTLED TDSTTRELNQ TAKQLQTHLT RLRMRPLSDL VGRFSRALRD LSLQYGKQVE
LKVVGKGTLI DRTILEALSD PLMHLVRNAF DHGVEDVKAR EMQGKPRTAV IEIKAAHRGN
QTIITVSDDG KGINLNKIRA KAEAMGLDAE LLAAASEDDL LSLIFEPGFS TAERVTDLSG
RGVGMDVVRN NLKQIRGDIR VDTTPGQGTT FTLTVPFTLS VARVLLVESN GMLLAFPTDV
IEEMLLPTVG QVYKTPGSEV LKWEGEMVPL TRLDEWLTFY CPRRVTTPEG VPSIGEPTVL
MVSLGEQLHG LVVDRCWGER EVAIRQVSGP LVMPPGFASC TIQGDGKVVP LVDAASLLRW
VKSERAPTER GVGAGEWGLG TSQEDKRNLT LHSSGDETKA IPNPQSPISN PQSPIAQSQK
DTILIVDDSI NVRRFLALGL EKAGYLVEQA KDGQDAVEKL LGGLMVSAVI CDIEMPRLDG
YGFLARIKSD PAFNELPIAM LTSRSGEKHR QLAITLGAAA YFSKPYNERE LLTTLREVIT
ESRGILPIPS GVR
//
