ID A0A327X272_9GAMM Unreviewed; 751 AA.
AC A0A327X272;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=B0I24_103224 {ECO:0000313|EMBL:RAJ99224.1};
OS Aliidiomarina maris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Aliidiomarina.
OX NCBI_TaxID=531312 {ECO:0000313|EMBL:RAJ99224.1, ECO:0000313|Proteomes:UP000249203};
RN [1] {ECO:0000313|EMBL:RAJ99224.1, ECO:0000313|Proteomes:UP000249203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.15366 {ECO:0000313|EMBL:RAJ99224.1,
RC ECO:0000313|Proteomes:UP000249203};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) 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:RAJ99224.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QLMD01000003; RAJ99224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A327X272; -.
DR OrthoDB; 9812358at2; -.
DR Proteomes; UP000249203; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; 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; 3.30.450.40; -; 2.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal 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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 384..603
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 625..742
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 347..377
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 675
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 751 AA; 83671 MW; B82561A0DC6E9607 CRC64;
MTESTPTHTS SQQAKDEAAR LKALRETGLL DSESSAEFDQ LTQLCQLLFD VPIVAVSMVD
EARQWFKSQV GLSVCETPRG VAFCDHAVSA REHIEVHDAA ADARFKANPL VTGAPHIRFY
SGFPIFSEQG HVLGTLCIID TKPRTLTSKQ RELQRLLTRQ AEVLVRRYDE QSQLMATQAR
LEEQDKLLQV LLTGLTDYSA LMSGDRLWTF LEQALRDLTD SQYALIGECI AGTKKLKIHA
ITDLSWDEPS RRLLEQLRAG QMTLSNPDTM LGQVFAQGQT LISNEFAQDP RRGGQPEGHP
PLHNYVGVPI MDGDEILGMF ALANSSEAFS QQTVGRLKPF TATCALLIRL YRQLEERERA
NKELQQAKDA AETASRAKND FLSSMSHELR TPLNSVLGYA QLLVNSKKQP LPERQRNQVE
QIYKSGQHLL ALINEVLDLA KIEAGQIPLS IESISLHDAA TEAVNVVQSI SGQYGVRVEF
DPRILPKVRV DADYTRTKQV LMNLLSNAVK YNREGGYVRL HWALNGELVH IQVKDNGIGI
AKDKISQLFQ PFNRLGAENS SIEGTGVGLS ITRTLTELMA GNIEAESVEG EGTVFHVTLP
MSKQQDTSID ELKAGSDAEF DRHIRVLYIE DNPANQRLME DIFSEHDNFE LTCAHDAQLG
LQLARQLMPE LILMDINLPG LNGFEALEQI RMDESLQHIS VAALSANAME KDVRRGLDQG
FDAYLTKPLA VEELYDLLQH IEAKHDDASS S
//
