ID J2IJ67_9ALTE Unreviewed; 535 AA.
AC J2IJ67;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=AEST_03800 {ECO:0000313|EMBL:EJI86834.1};
OS Alishewanella aestuarii B11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1197174 {ECO:0000313|EMBL:EJI86834.1, ECO:0000313|Proteomes:UP000012043};
RN [1] {ECO:0000313|EMBL:EJI86834.1, ECO:0000313|Proteomes:UP000012043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B11 {ECO:0000313|EMBL:EJI86834.1,
RC ECO:0000313|Proteomes:UP000012043};
RX PubMed=22965096; DOI=10.1128/JB.01255-12;
RA Jung J., Choi S., Chun J., Park W.;
RT "Genome Sequence of Pectin-Degrading Alishewanella aestuarii Strain B11T,
RT Isolated from Tidal Flat Sediment.";
RL J. Bacteriol. 194:5476-5476(2012).
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:EJI86834.1}.
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DR EMBL; ALAB01000002; EJI86834.1; -; Genomic_DNA.
DR RefSeq; WP_008606653.1; NZ_ALAB01000002.1.
DR AlphaFoldDB; J2IJ67; -.
DR PATRIC; fig|1197174.4.peg.371; -.
DR Proteomes; UP000012043; 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; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
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; PTHR45528; SENSOR HISTIDINE KINASE CPXA; 1.
DR PANTHER; PTHR45528:SF9; SENSOR HISTIDINE KINASE YRKQ; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
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; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EJI86834.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 195..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 306..526
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 535 AA; 60421 MW; ACB65DB3A39BE7E7 CRC64;
MFLRKLAVSL CVLLSIILLQ AGMAFWAQQN SEFHTERNRV ANQMLAEFIS LRADKQRLKV
WLAEYLLTED ANTQFRDTLF ARMQQQLTTL EQLAIRDQLY HTTETDLQHT MQQVKVISLL
QTNLQTLEQA LKTREIARYK DDAERWTALI SLFDKIQDTD LAELLQQAIA GQRQRAQSTE
SDALRAVQSV KRTTILISLL GLILAVMLGF YLARALSRPL QSLLDGTKQL QQGHFEYRIA
EQGPGEFAEL ARQFNLMSGY IADYAKREKQ SQLAAEQLVA ERTSQLQQAL DQLHQAEYRQ
KQLLADISHE LRTPATSIQG EAEISLRGQP KSTSDYQDAF SRILSASQQL SRRIDDLLLL
ARGEDRLRQV QLHTKPLAQF IQQSISTIQQ WLPAAVPLHT DISGRTADPL YLLVDDEKFS
AVLRIIVDNA RQYAKDSPAL NLKFCATETE LQLTLADQGI GIQPDEIAQV FARHYRSSAA
RQARPDGLGI GLCIAKDIME AHDGSIRLSA NQPRGTCVTL TLPLFPGVND EDSDR
//
