ID K9SLE8_9CYAN Unreviewed; 1207 AA.
AC K9SLE8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-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=Pse7367_2368 {ECO:0000313|EMBL:AFY70629.1};
OS Pseudanabaena sp. PCC 7367.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pseudanabaenales;
OC Pseudanabaenaceae; Pseudanabaena.
OX NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY70629.1, ECO:0000313|Proteomes:UP000010386};
RN [1] {ECO:0000313|EMBL:AFY70629.1, ECO:0000313|Proteomes:UP000010386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY70629.1,
RC ECO:0000313|Proteomes:UP000010386};
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 Pseudanabaena sp. PCC 7367.";
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; CP003592; AFY70629.1; -; Genomic_DNA.
DR RefSeq; WP_015165585.1; NC_019701.1.
DR AlphaFoldDB; K9SLE8; -.
DR STRING; 82654.Pse7367_2368; -.
DR KEGG; pseu:Pse7367_2368; -.
DR PATRIC; fig|82654.3.peg.2768; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG3087; Bacteria.
DR HOGENOM; CLU_281423_0_0_3; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000010386; Chromosome.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00088; HPT; 2.
DR CDD; cd00156; REC; 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; 2.
DR InterPro; IPR036061; CheW-like_dom_sf.
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; 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; PF02518; HATPase_c; 1.
DR Pfam; PF01627; Hpt; 2.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00073; HPT; 2.
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; 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFY70629.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000010386};
KW Transferase {ECO:0000313|EMBL:AFY70629.1}.
FT DOMAIN 7..113
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 280..386
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 760..895
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1072..1187
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 545..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 326
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 1122
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1207 AA; 132353 MW; 62C9A35370A376A6 CRC64;
MSSPDAEAQL QQELRHLFEV DTQKYLQLYV DTLAQLSDRT WKEDIQQIYR SVHTVKGGAV
TVGAEAILLV ATALEDLLSD LRYLDQAPPL ADGELKNVLQ EGGELLVASV QLEASSAAIV
VQRINDLRTN VQQRYLPDWS EQSQLYQEFA EQGFDLVVLD LDMALEQLPA QGEVAAEVID
VAQQTMTQLT QIGAEMELAQ GWQALLAQSK HIFDRPDCNH WRQTWPEYLQ HLKESAKNGG
KEVISQVSEA TISAPNLIQT EEAVTPIAFA QTNAQTNTAI DPAAAELLEL FRLDTQKDIN
TYFRTVDSLS ETTWQQDIQQ LYRSIHTIKG GAVTVGADAI LQTAKVFEDL LSDLRYAEQA
PPLADGNLQE ILQELGELLV SALQMGAERS PDATVARIQQ LHQQVSSTYL AEIDAQKQLA
IEFANNGFDL VTLDLEMGVE QLPAAGDVPE KAIETATQTI AQLREIGDDL QFASDWQALL
NQAESFATDA NQNNQTWQQE WPTRLKQLKE CARNVGKLPQ KSKPVTPALP EPEVPAAKPM
VTLTRPTTNA PGQLPLPPKP LRQSAKSATT PETRPAAEVQ IPVPLERLDR SSQYLIETLM
ATRATQGFYQ QVYAQLVPLV ALAQDGVRYI TQLREVQDDF ALTETNNDPA GSPQVERYRQ
GYTAINRLLE ISLRLTELGA ETGEAARRTI ESIESIDRSL RGLQQTIEES RLVPFESLAL
RARGILRDLT IRVGKPARLE VIGAKLELDA GTLRNLEPVL LHLIRNAYDH GIEAAEERSR
LGKPATGRIE LSLVRRGSLF VLTITDDGGG IDPEQITKAA IAKKLPLTDT SSPDKLLAVI
CQPGFTSTTA VSDISGRGVG MDVVQSQILE MGGQLSLRTQ LNVGSSFVMQ LPVPHLFVRC
MLLQAGDRTF AVPTSEVFTT MLLGDLLWQK TTPSQAPLYP ITVMEETGPV PALDLSQYWQ
GIPNPRSAIP TAIAVRTKRP DSLEGIWLVA DNMLGQSDLL VNSLPDPLFA PIGMIGVSLQ
SDGRLIPVID APALIEALLS QASGDLVVTQ PETEVTKTAA IAGDMSGLRA RQILVVDDAA
LMRRRLEGSL SGQGYSVVTC SDGLEAWQWL QAHVPPALVI TDIEMPGMDG FTLIDRCRQS
GLQMPILVVS SRLAEEWSKE TQRLGATDYL TKGFTTPDLL EKVATLIEEA AEQSEQLGDR
QPAPLNS
//
