ID B0C2A5_ACAM1 Unreviewed; 424 AA.
AC B0C2A5;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=AM1_3567 {ECO:0000313|EMBL:ABW28557.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW28557.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW28557.1, ECO:0000313|Proteomes:UP000000268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBIC 11017 {ECO:0000313|Proteomes:UP000000268};
RX PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA Blankenship R.E., Touchman J.W.;
RT "Niche adaptation and genome expansion in the chlorophyll d-producing
RT cyanobacterium Acaryochloris marina.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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; CP000828; ABW28557.1; -; Genomic_DNA.
DR RefSeq; WP_012163952.1; NC_009925.1.
DR AlphaFoldDB; B0C2A5; -.
DR STRING; 329726.AM1_3567; -.
DR KEGG; amr:AM1_3567; -.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_72_3; -.
DR OrthoDB; 438185at2; -.
DR Proteomes; UP000000268; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF42; TWO-COMPONENT SENSOR PPRA; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:ABW28557.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000268};
KW Transferase {ECO:0000313|EMBL:ABW28557.1}.
FT DOMAIN 5..128
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 184..415
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 130..157
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 62
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 424 AA; 46623 MW; C829415115BD149D CRC64;
MPKPIIVCVD DEIAVLDSLR RELSEVFEDT CEIETAMGGK DAIALVHDLI EDECDLSVII
ADYLMPDIKG DAVLQQVHQL SPQTLTIMLT GQANVDGISN AINTAQLYHY IAKPWQPEAL
QLTVREALNR YQLSKKIKDY QQTLERKVEE RTQELSETLH TLQTTQSELI QAEKMAALGQ
LVAGVAHEIN TPVGNALLAA SVLNNETSSL TQAFEQGALK RSALVGYLQT AQESSDLILQ
NLHGAAALIQ NFKQVAVDQT SHEQREFQII PYIESVLTNL EPKLKRTRHT VTVSGDAALK
TTSYPGALSQ VVTNFVMNSL MHAYQPGEAG QLKFEVTQQQ DRIILEYTDD GCGIPAEHQP
KIYEPFFTTG RDRGGSGLGL HIVHNLVTQS LGGTLSCQSE VSVGTQFMLQ LPLTLRKGEA
HARG
//