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Database: UniProt
Entry: A0A1M6A6W0_9RHOB
LinkDB: A0A1M6A6W0_9RHOB
Original site: A0A1M6A6W0_9RHOB 
ID   A0A1M6A6W0_9RHOB        Unreviewed;       763 AA.
AC   A0A1M6A6W0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05444417_0267 {ECO:0000313|EMBL:SHI32222.1};
OS   Wenxinia saemankumensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Wenxinia.
OX   NCBI_TaxID=1447782 {ECO:0000313|EMBL:SHI32222.1, ECO:0000313|Proteomes:UP000184292};
RN   [1] {ECO:0000313|EMBL:SHI32222.1, ECO:0000313|Proteomes:UP000184292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100565 {ECO:0000313|EMBL:SHI32222.1,
RC   ECO:0000313|Proteomes:UP000184292};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FQYO01000001; SHI32222.1; -; Genomic_DNA.
DR   RefSeq; WP_073325849.1; NZ_FQYO01000001.1.
DR   AlphaFoldDB; A0A1M6A6W0; -.
DR   STRING; 1447782.SAMN05444417_0267; -.
DR   OrthoDB; 9776727at2; -.
DR   Proteomes; UP000184292; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 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   Gene3D; 3.30.450.20; PAS 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; IPR017232; NtrY.
DR   InterPro; IPR045671; NtrY-like_N.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF19312; NtrY_N; 1.
DR   Pfam; PF00989; PAS; 1.
DR   PIRSF; PIRSF037532; STHK_NtrY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 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   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SHI32222.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184292};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          335..388
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          400..435
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          525..752
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   763 AA;  84357 MW;  1C18C661A1D96A0B CRC64;
     MRPRTPTSGG LSSYIRPGHT LTRIDRWRRQ RRTQTFFTLA LVVLGPILAA ATWFVLGPLD
     QGSTAPMLRI VLLGDFVYVS VVAAMVLRRV AQMIAARRAR SAGSRLHLRL TGAFALLALI
     PTVTVAVFSV LTINVGLEGW FSDRVRNVVG SSLAAAQAYE EEHRVELTRD ARALAQQLDE
     ARRENFFMSE GELRQALGRM EGQIQRDLSE VFVIDGTGAI RVRGARSYEF DYERPPEGLF
     AEVEGGGLAI VEDWDNNEFR ALLPLDSFVD RYLWVSREVD GEILGLLDDT QETVALYEQL
     EADRGRLLFE FGLLYMGFAA LLILAATWLG LWFAERLSRP VGRLVSASQR VGAGDLDVRV
     IEEEGDDEIA QLGRDFNAMT AQIRAQRQTL IDSAAQIERR RRLFDSVLSS VTSGVVGLDE
     SGRVTFANRS ARRLLYVGEA QEDMALSVAV PEFAALFEQL RTEAREVVQE QVNLVRGGKQ
     ESLLVRMSQR MAEDGELEGY VVAFDDVTDL VSAQRMAAWG DVARRIAHEI KNPLTPIQLS
     AERIKRKFRP EVSEADKLDQ MTDVIVRQTN DLRRIVDEFS KFARMPEPDR MRGDLAEILR
     DAVALQEAGQ PEVAFDSRVP EGPAWADLDS GMISQALTNL IKNAGEATES RIEAGAPEGY
     VPRIRVTMST GPSEAEIAIE DNGIGLPEDR ARLFEPYVTT RAKGTGLGLP IVKKIIEEHG
     GTLVLEDAEA FGAEGGDMHR GARAVIRLPL AQVLAPEAET SAA
//
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