ID K9VKI2_9CYAN Unreviewed; 1775 AA.
AC K9VKI2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, 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 ORFNames=Osc7112_3372 {ECO:0000313|EMBL:AFZ07750.1};
OS Oscillatoria nigro-viridis PCC 7112.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ07750.1, ECO:0000313|Proteomes:UP000010478};
RN [1] {ECO:0000313|EMBL:AFZ07750.1, ECO:0000313|Proteomes:UP000010478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ07750.1,
RC ECO:0000313|Proteomes:UP000010478};
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., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL Submitted (MAY-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; CP003614; AFZ07750.1; -; Genomic_DNA.
DR RefSeq; WP_015177015.1; NC_019729.1.
DR STRING; 179408.Osc7112_3372; -.
DR KEGG; oni:Osc7112_3372; -.
DR PATRIC; fig|179408.3.peg.4146; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_6_2_3; -.
DR Proteomes; UP000010478; Chromosome.
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; 1.10.287.560; Histidine kinase CheA-like, homodimeric domain; 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; IPR037006; CheA-like_homodim_sf.
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 Kinase {ECO:0000313|EMBL:AFZ07750.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000010478};
KW Transferase {ECO:0000313|EMBL:AFZ07750.1}.
FT DOMAIN 2..109
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 1233..1472
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1473..1618
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 1647..1764
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 495..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1096..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1203..1222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1204..1222
FT /note="Basic and acidic 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 1697
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1775 AA; 191053 MW; 680FBB495807AFFC CRC64;
MLPEQQQRIM GYFIEEAKDH LNTIEQGLLN LQTTIEDPEL VNEVFRAAHS VKGGAAMLGL
TSIQQTAHRL EDSFKVLKEC SVKVDQQLES LFLRIFDTLQ GLLEQLSGPF GLTEELGEQM
VRELEPVFEE LNGHLGGLVG HGEYHPDESI ALAVPEPVMA GIGVGAFASS RSFPDSPSVY
APDVRETEDS ALQLVFDSDV PARMRELLQE FKQPEGPESR RQLKNICQNL LGTGEQFELP
CWIELIQAVS KAIANPENTY RTLAPTVIKD IKQAQELVIS GLESSIVPSA KLLSLLPAVQ
VPETDFEDLL AFAQPSKSGT NVVSVEDEAW ELVGSGDVPD GLNKLLPTIS GVSIDELFDQ
LDSGDSNDDS GIRSAQFDED SAFAESDIET SAFRGSTRTG PEVGAAELNT LADLFDGESP
DLDGAWEEEE DLDYAQSSGI SAGMLGSDDD NSGDFTDLLF DEYDDTESSE TKTTPPIDDL
TSLFGEDVLF GEEAEGSAVA AGQTNAGSSQ GLTRQQLKTG NGRGGERRDD TAAPARGQAD
EDALGTLLDE VAAQTSAGVT DNADFDNLFG DLGLSEATGV PAVSSEYSLK SEALDGESQE
PAAGGGNSDS ADAEALALPV MDDFESISEL GEDSDLSELL GITSNFLSSE DEGEENAGDR
DRVAGIAQNE ERGNVLNMTS NSDLDISADE NWLEDAFGME DESVQSLNLD LDDTDLDALF
GDMTSGAISE DEQTVRDRQG ATTSREAADL AELFGSVPTG TEYDGEASGQ ALGGWPNDGN
SELLSAGVGV DEGDLGSLFE NNGAAVSDQG LTNSAEVEFG ALSDDRPESE ISNVESDEAA
AFDFLEDMFG EGMVHPGDAG AAPDDGATVD VKELSAQPAG DLFDELGADL FDRAEIDVAG
ESEGEDDLFN ALETDFLSAD LEPLPAESLD GMFEGDADLL SAMETGATLN NSILMGFDDL
LDSIDAEVLV TSELTTGFWD AEDESAQPDS SELEEGSLAD FFGEAESGDE DAEEGNFDDL
EALLIAGGAG AVIAASGSTN QSPVNTEVFS DLEELLSESA TMPEIHGLPA TTASKAPRAA
ADESDDEFGD LEKLLEEPKD GGRQGEGNMG PSAINRPRRN ARAGGFGDQT MRVPVKQLDN
LSNLMGELVV NRNSLEQDQE RMRQFLDNLL HQVTLLSDVS QRTQDFYERS LLEIALLANR
QGHRSGWRSE DAAPTRDSTR DSAWRPEEMD RFTPFHSLAQ EIIELIVRVR ESAADIEFLV
DEADQVTRQL RQVTTQLQEG LTRARMKPFA ETTDRLFRAV REIAIKCGKQ AQLQVEGKDI
LIDKMIVDQL YDPMTHLVNN AITHGIEAPE VRLAAGKPAV GRITIRAFHQ GNQTVVSVSD
DGAGIDPQRV KAKAIKQGML TAAQAQRMSR SEVYDLLFMP GFSTQEQATE YAGRGVGMNV
VQTSLQEIRG TVSIDSTIGK GTVFTIRLPL VLSISKALTC ISDRARIAFP MDGVEDMIDV
PRDQVTTGAD GLPCIEWRGQ SLPFRPLRDL LAYSRHLGRG SVYGFNTDDD MISVIVLRSA
GNFLAVQVDQ VSTEQEIVIK PLEGPVPKPI GIAGATVLGD GRIVAIADVL ELIDLATGRL
RKDTGGTLWD EGDRAAAEAE IEKTEPTVLI VDDSITVRSL LSITFEKSGY RVEEARDGKE
AWEKMKSGLP CDIVFCDIEM PRMDGLELLS RMQKDAVLCE LPIAMLTSRG ADRHRQMAYS
LGAKGYFTKP YLEEQLLDAA SRMLKGEVVG APVGV
//
