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Database: UniProt
Entry: B0C2A5_ACAM1
LinkDB: B0C2A5_ACAM1
Original site: B0C2A5_ACAM1 
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
//
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