ID B0CAG9_ACAM1 Unreviewed; 1053 AA.
AC B0CAG9;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=AM1_4054 {ECO:0000313|EMBL:ABW29035.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW29035.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW29035.1, 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; ABW29035.1; -; Genomic_DNA.
DR RefSeq; WP_012164388.1; NC_009925.1.
DR AlphaFoldDB; B0CAG9; -.
DR STRING; 329726.AM1_4054; -.
DR KEGG; amr:AM1_4054; -.
DR eggNOG; COG0643; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR HOGENOM; CLU_000650_2_1_3; -.
DR OrthoDB; 291966at2; -.
DR Proteomes; UP000000268; 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:ABW29035.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000000268};
KW Transferase {ECO:0000313|EMBL:ABW29035.1}.
FT DOMAIN 1..108
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT DOMAIN 547..756
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 758..904
FT /note="CheW-like"
FT /evidence="ECO:0000259|PROSITE:PS50851"
FT DOMAIN 929..1046
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 382..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 487..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
FT MOD_RES 979
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1053 AA; 116070 MW; 34B887E0AC142591 CRC64;
MQPEQQRIMV YFIEEAKEHL NTIEHGLLNL QTVVADPESL NEVFRAAHSV KGGAAMLGIH
SMQHISHRLE DYFKVLKEHD LPVDQKLESL LFKSFDALHI LTEELEQSFG LSDELSAKTL
SEIDPVFAEI DSHLTEIAGP GVDISALLSD APAPKPQTTT AEPEVLDAQC LEIFQTDILQ
YLREILGLFK QPDTPENRQT LAKICQDLGQ VGQEFKLKGW SELLEVAGVV VTHPSNSFAT
LAGVIVPNIK EARDLVLAQR AADVKPMPAL LDLMPALDFG DLGITDSAET ETEDWLDIFA
DDDTSASTDA DKGGSFLDDL FNEPALNFDT STNADVPEPV AAADTNFANL DTLLAETSTQ
EATTPTVAQS EDDFDDLEKL LEEPSRPAKA KPQAKAPQKR TGTKPLRRGS AIAQTMKVPV
KQLDNLGNLI GELVVSRNSL EDSQNRLRQF LDNLLLQVQQ LNDLGRNMED LYERSLLENS
LLSSRQQQAV ASGNGGNGNS GHSTGQQFDA LEMDSFTGFH TLSQEMIERI VRVREAASDI
EFIVGGTEQV TRMFRQITTQ VQEGLTQSRM VPFSQVAERL PRAVRDISMK CGKKARLELE
GRDTLIDKSI LERLYDPLTH LVNNALFHGI EAPDVRQSLG KAEEGVIKLR AFYQGNQAVI
SIMDDGAGID VERVKAKAVQ KNLLTQDEAD NLSRQEAYAL LFKSGFSTQD QANDLAGRGV
GMDVVRNSIH EIRGVINTDS GIGKGTTFTI RLPLTLSITK ALCCIDNSTQ MAFPIDGVQD
VIDLPKEQLQ QDADGQVLVT WQDKQLPCKP LGELLAYNRR FKRSSSYNAS NTKDDGMASV
VILRSADDLV AIEVEQVLAE QEIVIKQLAG PVPKPMGIAG VTVLGDGGIM AIADVMELVD
LCLDRLEVNS NLWKSILENT EVEEDTDPMV LIVDDSITVR ELLSMTFNKV GYRVEQARDG
QEAWEKLRSG LPCDLVFCDV EMPRMDGLEL LSRLQQDDDL QDLPVAMLTS RGAARHKQMA
TELGAKGYFT KPYLEEVLLE AAQRMLNGEV LVK
//
