ID I3YZU2_AEQSU Unreviewed; 1302 AA.
AC I3YZU2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Aeqsu_3072 {ECO:0000313|EMBL:AFL82510.1};
OS Aequorivita sublithincola (strain DSM 14238 / LMG 21431 / ACAM 643 / 9-3).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aequorivita.
OX NCBI_TaxID=746697 {ECO:0000313|EMBL:AFL82510.1, ECO:0000313|Proteomes:UP000006049};
RN [1] {ECO:0000313|EMBL:AFL82510.1, ECO:0000313|Proteomes:UP000006049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14238 / LMG 21431 / ACAM 643 / 9-3
RC {ECO:0000313|Proteomes:UP000006049};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Goodwin L., Pitluck S., Peters L.,
RA Munk A.C.C., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA Ovchinnikova G., Zeytun A., Detter J.C., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA Faehnrich R., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Aequorivita sublithincola DSM 14238.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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; CP003280; AFL82510.1; -; Genomic_DNA.
DR RefSeq; WP_014783759.1; NC_018013.1.
DR STRING; 746697.Aeqsu_3072; -.
DR KEGG; asl:Aeqsu_3072; -.
DR PATRIC; fig|746697.3.peg.3131; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG2207; Bacteria.
DR eggNOG; COG3292; Bacteria.
DR HOGENOM; CLU_000445_28_1_10; -.
DR OrthoDB; 358279at2; -.
DR Proteomes; UP000006049; Chromosome.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17574; REC_OmpR; 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 Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR020449; Tscrpt_reg_HTH_AraC-type.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 4.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00032; HTHARAC.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 2.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Kinase {ECO:0000313|EMBL:AFL82510.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:AFL82510.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1302
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003684164"
FT DOMAIN 810..1022
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1055..1170
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1201..1300
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1103
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1302 AA; 148657 MW; 52EEEBA6617119E4 CRC64;
MNPLKLLFLL MLPCFALSQN NKQVAFRELT VEQGLSQNSV VSIAQDSTGY MWFATQDGLN
KYDGRAFTHF DIQFEDVTRP TFSKLGEIYV AKDGDLWIVS NSGRLEKYNP ENVNFKAIKS
VNNVSTLIQD EAFNYYLGTY ENGIYKINHK NGDTLQFLKP EDSKRTIYDF LELYNNTILA
TTDNGFFIIN NDSYEFQPIR PETNFSTITQ SQNNTFYLGS YGKGLFIKQR NEADFSQFKG
FKNAEIPEDL IIQDLLVDKR NQLWIATYGR GVYLVNFEKQ TIQNFTENKN NPYALHYNDV
LSLFEDNTGT VWLGTDGTGL SYYDEYLIKF NVLTNDQVPL NVNVDVIRAI TNDTENNTWV
GTSGKGLTRF NIDKQDFYTY TTQNSDLLGD RIMSLLFDER ILWIGHQTHG LQMMDAKGKI
TSFKETALFT IWKIYKDKNG ALWLCTRDHG LLQFDKNKGI IQQFTIENSN LSTNNIRTVE
QGKEGELWIG TETDGLFKLN TQTNSIENVE IVNGNIKSLY FNGSDLLIGT NGDGLQILNT
NAITAGKQEK AIKKYKTAEG LPNNVIYGIL PDNEGYLWIS SNKGISKLKF EENSISVIDN
YSNYDGLQAF EFNTGAYFKD KNGMLYFGGL AGINWFNPNQ LSFNPIQPKT VISGFDVFNK
SRNLTPNQNL KYDENTLTFT FSSLHFSQPE RNEYRYKLIN NDADWIAAGN TNLAHYTNLP
PNDYEFQVIS SNYDGVWNME PATYSFTILK PWYTTNLAKV FYLLLFLSFA FYLYRYLKWR
WEIKTQLQLE LEETARLKKL DELKTKLYTN ISHEFRTPLT LISGPIDNQL AKPEISERDK
MELSLVKQNA ERLLNLVDQM LELSMIDSGQ RKLAIQQGNL SVLLKQIVSA FQYKANQKRI
TISSKINDLN SVWFDKDIIE KVTSNLFSNA VKYAPIDSII VFEANKQEGM LVLSVINESD
SISKKDLSKL FQRFYQDNKL SEGVGVGLAL VRELIALSKG SIIANNIDDD RIQFTVSLPI
NKEAFEDEVI ITNEEAITET EIVQTINISN KEKPLLLIVE DEADIRAFIS SIFKYNYQVS
EAENGKIGVE KALKDLPDLI ISDIMMPVVD GIELCNTLKK NELTSHIPII LLTAKVGEEN
EIEGIKTGAD VYVTKPFSSE KLKIRVEKLI ENRRNLQKHF SKTLSINPEM AITSTESDFL
IRLQKVLDGH ITNSEFTSDS FGKLMLMSRT QLHRKLKAIT GMSTSEFIRS QRLKLAVDLL
RKSDANVSEI AYQVGFNTPS YFGKCFKETY GCTPNEYLSN NL
//
