ID A0A023C063_9FLAO Unreviewed; 677 AA.
AC A0A023C063;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ATO12_02715 {ECO:0000313|EMBL:EZH75722.1};
OS Aquimarina atlantica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=1317122 {ECO:0000313|EMBL:EZH75722.1, ECO:0000313|Proteomes:UP000023541};
RN [1] {ECO:0000313|EMBL:EZH75722.1, ECO:0000313|Proteomes:UP000023541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S11-z7 {ECO:0000313|EMBL:EZH75722.1,
RC ECO:0000313|Proteomes:UP000023541};
RA Lai Q.;
RT "Aquimarina sp. 22II-S11-z7 Genome Sequencing.";
RL Submitted (APR-2014) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EZH75722.1}.
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DR EMBL; AQRA01000001; EZH75722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A023C063; -.
DR STRING; 1317122.ATO12_02715; -.
DR eggNOG; COG4191; Bacteria.
DR OrthoDB; 9810447at2; -.
DR Proteomes; UP000023541; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.60.40.2380; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR011623; 7TMR_DISM_rcpt_extracell_dom1.
DR InterPro; IPR011622; 7TMR_DISM_rcpt_extracell_dom2.
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 PANTHER; PTHR43711:SF1; HISTIDINE KINASE 1; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF07695; 7TMR-DISM_7TM; 1.
DR Pfam; PF07696; 7TMR-DISMED2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000023541};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 308..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..386
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 452..670
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 677 AA; 77721 MW; DCD9C2E9800ABDDF CRC64;
MTTYFKYYFG LLLIILLSPL NSFSQTTILL DDSTELHDIG KQTYYLEDTS LKLSIEEIIN
STLETKYKEY TQETINFSST ASAYWLKFRI TKTIPGDFYL NVGSAFIDSI SLYEFDDKNQ
LISTRHTGDD LPFNTREIEV GNYLFALDFD VNNTRTFYLR VKSDQPLFFP LRVGTLPNFL
NYEHDLDFLQ GIYFGFMLLI FLYNLFLYFS TREKIYLYYI AYVFSITWFM ASVFGYFFEY
FWPNTPFINQ IVVVSSGLTM ITATLFTQKF LNTKESGSMM HKGSMVFLII GILICALVLL
GFKIEGLKLS QGGLLIMASY FLILGIRFKL KGYRPAKYYL LAWGALIIGI CFAILESLNL
TFVMTYLNAM QIGSALEVLL LSFALGDRIN MYKKQKEDAQ LEALLAAKEN ERLIQEQNVI
LEKKVKERTA EVAIRNEELV NLNKEKDMLV NIVAHDLRTP LSHIRLLIQL IDVTSLDLTK
DQVSYLTEID NSADRLSQMI GRILNIHALE TNRVKLKNQI IDLVELVNYV VRCFRLTAED
KEIKMITTSQ PGDHFVEVDK NYMIQVLENL VSNAVKFSER GSEVILHVKS QDARTYVVVE
DQGPGISKED QKKLFGRFQR LSAQPTEGEA SIGLGLSIVK KYIESMDGEI HCESELGIGT
KFIISFDSKD HLEKIES
//
