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Database: UniProt
Entry: A0A1H7ZTH4_9RHOB
LinkDB: A0A1H7ZTH4_9RHOB
Original site: A0A1H7ZTH4_9RHOB 
ID   A0A1H7ZTH4_9RHOB        Unreviewed;       841 AA.
AC   A0A1H7ZTH4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN04488103_101642 {ECO:0000313|EMBL:SEM61730.1};
OS   Gemmobacter aquatilis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Gemmobacter.
OX   NCBI_TaxID=933059 {ECO:0000313|EMBL:SEM61730.1, ECO:0000313|Proteomes:UP000198761};
RN   [1] {ECO:0000313|EMBL:SEM61730.1, ECO:0000313|Proteomes:UP000198761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3857 {ECO:0000313|EMBL:SEM61730.1,
RC   ECO:0000313|Proteomes:UP000198761};
RA   de Groot N.N.;
RL   Submitted (OCT-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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR   EMBL; FOCE01000001; SEM61730.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H7ZTH4; -.
DR   STRING; 933059.SAMN04488103_101642; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000198761; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
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; 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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF12860; PAS_7; 2.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198761}.
FT   DOMAIN          345..566
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          581..695
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          707..824
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         756
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   841 AA;  93183 MW;  97CE5F8FDDCCA52F CRC64;
     MDLSERLAKE RRARLAAERL LEQKSRELFA ANEKLALHAR SLSDQIVEQR QVVKSALSEA
     EALKGQNLRF LSDLERAHTA AVMAERRLWD SINTIRDGFA VFDSANRLVA ANRAYLAAFE
     SEDIAPGTAY DTLLRSACET GLVDIGSVPP QDWCSTMLAR WDQDPIEPLE LQFSNGTWVR
     LVDHRGRDGD MVSLALNITD QKRIWAAIEA IPDGFVLFDR EDRLMVCNQR YRDLFPESAP
     AMVPGATFET ILRYGLDRGQ YADAQGREAD WLDERLRLHE AKSSDFEQEL TPGRWLRVID
     KETPDGGRVG LRVDITRQRE QQAALQAARE AAEAAVRAKS AFLANMSHEI RTPMNGVVGM
     AELLCDTPLT EEQRLFADTI RSSGEALLVI INDILDYSKI EAERLTLRPE PFDLERVIHE
     VSMLLQPKAR AKGVDLLIDF DMFLPTRYIG DPGRLRQVLT NLIGNAVKFT DAGHVLIRVV
     GIAAEPGAQQ LHITVEDTGI GIAPEHLDHI FGEFNQVETD SNRKFEGTGL GLAITQRLVD
     RMGGAVWVDS ELGRGSCFGF RLSLPVAEIS EDHPATVSLK RALVVDDQYI NRTILERQLV
     TCGMQAVLCR SGADALAVLD SDRDFDVILC NQDMPELDGL TLVQRLRGAG IVAPVLLLSA
     NPAAARDLPG ADLVAHILQK PLLRADLYRR LQDLAPPPTA APLRQMRVLA AEDNRTNQLV
     FRKMVRDLDL DLTFAHNGRE AVALFTTLHP DLIFMDISMP EMDGREAARA IRQAEGTGPR
     VPIIALTAHA MEGDAETILA AGIDRYLTKP LRRSAICEAL VEFTPADVRP VLTDTPEAGA
     A
//
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