ID B0CDG5_ACAM1 Unreviewed; 1514 AA.
AC B0CDG5;
DT 26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=AM1_1870 {ECO:0000313|EMBL:ABW26890.1};
OS Acaryochloris marina (strain MBIC 11017).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Acaryochloridales;
OC Acaryochloridaceae; Acaryochloris.
OX NCBI_TaxID=329726 {ECO:0000313|EMBL:ABW26890.1, ECO:0000313|Proteomes:UP000000268};
RN [1] {ECO:0000313|EMBL:ABW26890.1, 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};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
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DR EMBL; CP000828; ABW26890.1; -; Genomic_DNA.
DR RefSeq; WP_012162392.1; NC_009925.1.
DR STRING; 329726.AM1_1870; -.
DR KEGG; amr:AM1_1870; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_248033_0_0_3; -.
DR OrthoDB; 474548at2; -.
DR Proteomes; UP000000268; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0009584; P:detection of visible light; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 4.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; IPR036641; HPT_dom_sf.
DR InterPro; IPR016132; Phyto_chromo_attachment.
DR InterPro; IPR013515; Phytochrome_cen-reg.
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; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 3.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF00360; PHY; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 4.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 4.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50046; PHYTOCHROME_2; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ABW26890.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000268};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 39..219
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 512..653
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 696..835
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 869..1093
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1119..1235
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1264..1378
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1410..1503
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 1168
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1313
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1449
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1514 AA; 169646 MW; 2254CA9CBCB7BEBA CRC64;
MDVSSSKLNA DCSYPDVPSK LTQQSLLNRI TTRIRQSLEL NEILSATVAE VRAFLGTDRV
KVYKFFPDGH GLVIAESIRE DHLPSLLGLN FPADDIPLPA RELYLKARQR SVVDLSTQQI
GFSPLNCTET GSELESRDIR FRPIDPCHVE YLKAMGVQSS VVVPIVIEQS SLEQIQSESE
VVSGLNQGQR LWGLLVSHHA QPRQVEESEL ELIQAVVDQM AVAIGQATLL DRVREQAVLE
AGVNHVTALL YTKPTVQLEV ALAEMVAVMQ GTGGRLYLSH TTSEQSAELY CCGDQPSTLD
HDRLIEENAL WQNYLNSTQS VDTPDTESRP WSVDWMRKNY ALSPQARSSA RSKTVWAIAD
IYREPLFRVL SPAFQSTPIR GVMILPLYFD KELLGCITIF RNEVEEELCW AGFHHPDSRQ
LAPRQSFEAW RQIKAGQSQP WTDAEVRLAE ALGERFSAAI NQYQLYQQVQ TLNTHLEEQI
KERTAELHRS TAIANQQRAL TNILSKLQKA LDLDTIFQTT TQEAQRLLDV DHVAVYQFDE
NWGGSFINNF RAVKPEWEEV VYSTRDVWND SHLQETKGGR YRHNHVSVVN DVSKAGLSPC
HLETYHYYQI KAFLIAPVFV GSRLWGLIGA YQHSNPYEWK PLEVDFITQL ATHLGVAVQQ
AGATEKVQNQ AQQLAVIAEQ QHTLTNVISK IRESLDLETI FKTTTREVRR LLQVDRVVVF
QFLPDVQYSQ GEVIAEDVHP DYRSILGYDV KGDCFQDRYT ASPGTHQVFA IDDLNTCNLD
PCYVEMMQGL QVQAHLVVPL FRSNILWGLL AIHQCSAPRP WQVKEREFAI QISTQLGVAL
QQAEFLNQAQ QSKEAADAAS QAKSDFLAHM SHELRTPLNA ILGYVEIMQR DPQLGETQTE
HLGIIGRSGE HLLSLINDVL EMSRIEAGQL ALTQVSFDLY RLLDSLQDML EAKAKLQGLQ
LYFERSATVP QFVFADEGKL RQVLINLLGN GLNYTEKGQV LLQVDTPEQS GQPGRACQLT
FAVMDTGPGI KASDVDQLFE AFTQTDSGYR AQEGTGLGLP ISRRFVQLMG GDIEVDSTVG
QGSTFRFTIP VTLADAAEVH TVKPTRQVVS LAPGQPTYRL LLVEDKWANR QLMQQWLAPF
GFDIREAVNG EEALAVWQEW APHLIWMDMR MPVMDGYKAT REIKAQCGDN PPVIIALTAN
AFEEDRLYAL SVGCDDFVRK PCQESTILDK LAEHLGVQYI YSEPEPSESN SLEEVASIQP
EDLRILVADD NTLNQQLMVQ RLVHLGYSAD VVSDGQQVVA ACQTQMYDLI LLDVQMPKMN
GLEVVQTLRQ QEMCPYVIGV SGRTLPEEKQ ECLDAGMQDY LCKPVSLEDL KVALSQYHPP
SDLALPQAMK PALIEESAIQ ALIEIGGDDG GSFLVSVIDN FLRDAEPMLA GLKDAISTTN
YVQINEIAHS LKSMSASMGA TQLAHQLKEL EHMSKLENLA ISSTWMNKLE QEFEAVRLAL
TLEKQNYQTS AVSS
//
