ID L8M315_9CYAN Unreviewed; 780 AA.
AC L8M315;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Xen7305DRAFT_00024590 {ECO:0000313|EMBL:ELS02741.1};
OS Xenococcus sp. PCC 7305.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Xenococcaceae;
OC Xenococcus.
OX NCBI_TaxID=102125 {ECO:0000313|EMBL:ELS02741.1, ECO:0000313|Proteomes:UP000011203};
RN [1] {ECO:0000313|EMBL:ELS02741.1, ECO:0000313|Proteomes:UP000011203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7305 {ECO:0000313|EMBL:ELS02741.1,
RC ECO:0000313|Proteomes:UP000011203};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELS02741.1}.
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DR EMBL; ALVZ01000185; ELS02741.1; -; Genomic_DNA.
DR RefSeq; WP_006510132.1; NZ_ALVZ01000185.1.
DR AlphaFoldDB; L8M315; -.
DR STRING; 102125.Xen7305DRAFT_00024590; -.
DR PATRIC; fig|102125.3.peg.2955; -.
DR eggNOG; COG0643; Bacteria.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000011203; Unassembled WGS sequence.
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; 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; 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 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:ELS02741.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000011203};
KW Transferase {ECO:0000313|EMBL:ELS02741.1}.
FT DOMAIN 1..105
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 259..502
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 504..640
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 660..779
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 127..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 162..196
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 712
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 780 AA; 86651 MW; 75F8862D0C7B4F5C CRC64;
MFIEDTELRE LYKIASADHL EKIENGLIHL EKNPNDQDKL EELLRATHSL KGDSRMLGVE
EAEMLVHQME DLLSDIKENN SVFTSNLCDR LYHGLDAVRK IAREAVTGES SGISTFHVMA
QLMGAEDGAD PDSVAASQSA PETPEVNPEL LLANEQEAEF PAELLAELAK EQEAMAAAAQ
EKAQQELAKA AQIEDHQIET VRIGFPKLDA LMTQAGELSV TKLRLARRTE DLREIINLWE
DWSRAVFATQ LSIKELEQHL TSETLEPIQK FEQLNQEYLE QLGERVTQLK NVTVEDNARL
EIVAHSLETG IRDLRLLPLA NVFNLFPRMI RDLAKQLGKE INLKIEGGDI AVDKRILEEI
KDPLTHLIRN AIDHGIETTE ERIAQGKSAT ANLSIRGYQN SNSICIEVID DGRGLDTENI
KSTALRRGLH TESELAAMTT EQAQSLIFAS GFSTRIEVSE ISGRGVGLDV VRANIERLKG
SIQVSSTYGK GCQFQLTLKT SLSTTHILIV EVNRSIYAIP VDFIDSMLFV ERDDIFQVEG
TPTITVEGEP LSISWLSSLL KLPKSSDNNS MTKMSCVILK SGNERLGVIV DRLVDQQHII
LKPQSKLLRR IPNISGATIL GTGEICMVLN PKDLLQTALQ GTAINDELSG ILTQIRTKPK
VLLVEDSLPI RTQVRRILDS SGYDVTVAVD GLDGFQKLQA ADYKNFQAIV SDVEMPNLSG
LEMTARIRQD KEYNELPIIL VTTLAKESDK RRGADAGANA YLTKGDFDQT VLLDTLRRLI
//
