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Database: UniProt
Entry: A0A1B3W7A6_9GAMM
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Original site: A0A1B3W7A6_9GAMM 
ID   A0A1B3W7A6_9GAMM        Unreviewed;      1141 AA.
AC   A0A1B3W7A6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BGP89_05880 {ECO:0000313|EMBL:AOH35948.1};
OS   Luteimonas sp. JM171.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Luteimonas.
OX   NCBI_TaxID=1896164 {ECO:0000313|EMBL:AOH35948.1, ECO:0000313|Proteomes:UP000095036};
RN   [1] {ECO:0000313|Proteomes:UP000095036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JM171 {ECO:0000313|Proteomes:UP000095036};
RA   Wan X., Miller J.M., Rowley S.J., Hou S., Donachie S.P.;
RT   "Draft genome sequence of a novel Luteimonas sp. from coral mucus,
RT   Hawaii.";
RL   Submitted (AUG-2016) 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC       family. {ECO:0000256|ARBA:ARBA00006434}.
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DR   EMBL; CP017074; AOH35948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B3W7A6; -.
DR   STRING; 1896164.BGP89_05880; -.
DR   OrthoDB; 9764438at2; -.
DR   Proteomes; UP000095036; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd10322; SLC5sbd; 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; 3.30.450.20; PAS domain; 1.
DR   Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
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; IPR038377; Na/Glc_symporter_sf.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; NF041832; near_NosP_CTERM; 1.
DR   PANTHER; PTHR43047:SF9; HISTIDINE KINASE; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AOH35948.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000095036};
KW   Transferase {ECO:0000313|EMBL:AOH35948.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        67..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        158..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        187..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        272..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        321..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        367..391
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        403..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        436..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          790..1003
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1025..1138
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          752..783
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1073
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1141 AA;  125171 MW;  8C4F6510225ABB44 CRC64;
     MSNLVLLLVS LGYAALLFAV AWWGDRNPGF TQRPGLRPIV YSLALAVYCS SWTFYGAVGT
     AARNGIGYLP IYLGPLLLLL FGWRILERLA LIAQSQNTVS IADFIAARYG RSQRLAAMVA
     LIALLAAVPY LALQYKAVAL SLQVLGDELM PTGTFGDPAL YVALLMALFA GLFGTRQVDA
     TEHRPGMMLA IALESLVKLV ALVAVGVFAV FWFGGRELAL TRATSELLAN TPSVGFVGQA
     LLAFTAIICL PRQFHVAVVE CVDVRDIRRA RWLFGGYLVL ISLMVLPIAA AGASLFADGS
     VLADTYVLAL PLAEHREALA LFAYVGGFSA ATGMVIVASV ALAIMVSNDL VMPLLLRRGW
     AQEHGGNVAS TVLWIRRVAI LCFALLAYGY YRASGTDTAL ASYGLMAFAA VAQFAPALIG
     GLYWRGASRQ GVEAGLLVGF GVWIYTLLLP TLTDAGWLTP GWMAEGPFGI AWLRPRQLFG
     IEGWDPLTHG TFWSLLFNIG ALLLVSARWR PGLEERLRAA PFLDPYAQRR ALGASDWRGV
     PIADLQALAR RVVGASAAKR AFADFADSQG IELTPGTLAD RSWIQFTERL LAAAIGAASS
     RLVMTSTLRG SGMELAEVMA VLDEAGQELR FNREILSSTL ENIDPGVSVV DHDMRLVAWN
     RRYQELFDYP DGMLYVGRPV ADLIRYNAER GELGELSPEE IQEEIDKRIA YMAAGSPHSS
     ERTIGRGVVT DVRGQALPGG GYVTSYSDVT DYKRVERALR EINETLEQRV TERTREAEAA
     QQSRTRFLAA LSHDVLQPLN AARLFASALR ETDDPGEQQR LAERVDTSLR AAEELLDGLL
     DVSRLDAGAL SPEFTEFDAG ELLRELAAQY APMAAARGIE VKVRARALPV RSDRRLLRRV
     LQNFLANALR YTPKGRILMA ARPRGGKVAL QVWDTGPGIP EHHMRQIYDE FHRFRQPFDW
     DERGLGLGLS ICQRISRLLD HRLDAQSRVG EGSMFSILVD RAERAEPAHP APARLDMAEP
     LSGLRVLCVD NDPDILAGME ELLRRWQVHV ITASTVDEAV DGLAHDPEML LVDYHLHDRF
     NGLQTLELLR NARPHLAGAL VTADGSDRLK QEAREYGYRV LTKPVKPASL RAYLAAQVRR
     Q
//
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