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Database: UniProt
Entry: A0A0J5GHB3_9NEIS
LinkDB: A0A0J5GHB3_9NEIS
Original site: A0A0J5GHB3_9NEIS 
ID   A0A0J5GHB3_9NEIS        Unreviewed;       703 AA.
AC   A0A0J5GHB3;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=ACG97_06920 {ECO:0000313|EMBL:KMJ53701.1};
OS   Vogesella sp. EB.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Vogesella.
OX   NCBI_TaxID=1526735 {ECO:0000313|EMBL:KMJ53701.1, ECO:0000313|Proteomes:UP000054352};
RN   [1] {ECO:0000313|EMBL:KMJ53701.1, ECO:0000313|Proteomes:UP000054352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EB {ECO:0000313|EMBL:KMJ53701.1,
RC   ECO:0000313|Proteomes:UP000054352};
RA   Arrua Day P., Revale S., Alvarez H.M.;
RT   "Genome wide analysis of metabolism in the polyhydroxybutyrate-producing
RT   Vogesella sp. strain EB.";
RL   Submitted (JUN-2015) 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   -!- 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:KMJ53701.1}.
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DR   EMBL; LFDT01000008; KMJ53701.1; -; Genomic_DNA.
DR   RefSeq; WP_047966615.1; NZ_LFDT01000008.1.
DR   AlphaFoldDB; A0A0J5GHB3; -.
DR   STRING; 1526735.ACG97_06920; -.
DR   PATRIC; fig|1526735.3.peg.1482; -.
DR   OrthoDB; 9815750at2; -.
DR   Proteomes; UP000054352; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; 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; IPR013656; PAS_4.
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; PF08448; PAS_4; 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:KMJ53701.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054352};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        74..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        272..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          297..349
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          361..433
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          492..702
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   703 AA;  78248 MW;  50FD1D3099037E1A CRC64;
     MRYPVIATAF GFVLLYLLAI STGNTSKLAE YYWWVFGLNA FGLVGLLAVV ARQMLRLRRR
     VKSREFGAKL TQKLVVMFTL IALLPGMLVF TVSAQFLTRS IESWFNVEVE NALDRGLELG
     RNALGFVLSD LSRKSRLVAR DIADYSDHSL NSQLLRMREQ LGVQEIAVYN QQGRLLSFAG
     PDDVRYLPRA PDPDVLRSLR QRKSHEIIDS DPDGTLELKV LLSYRSYVND QTQIIQIIQP
     APVDIARDAE LIEDARAEYR QLVLSRDGLK TFYMLTLALV FLLALTAALA FALFISERLS
     APLSELAAGT RAVAQGDFSK RHPVYRKDEL GILTTMFNRM TQQLDEARLT ADESRRLLES
     GKLYLESILA NLSTGVIAFD YNWQLRAANT SASRILGVDF GELSGHELQV WPVLRPELSP
     LVETILREAA TTNPHDWQQQ IDYLGAQGAR QLVARGAILP EQPATGYVVV FDDITELGRA
     QRDAAWGEVA KRLAHEIRNP LTPIQLSAER LAMKLADKLQ PSDAEMLKRA TDTIIKQVTA
     LKGMVDAFRD YARAPKIKLV KLELNTLLRE VLVLYESNPA LKVDLSLQAL PVMGDAALLR
     QVLHNLLQNA QDAILDADIP MIQISTRLEG RNVLVCVEDN GVGFSPDILP RAFEPYVTNK
     AKGTGLGLAV VKKIVEEHHG QITLANAQSG GARILLTLPL LEA
//
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