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Database: UniProt
Entry: A0A1G8P9F2_9RHOB
LinkDB: A0A1G8P9F2_9RHOB
Original site: A0A1G8P9F2_9RHOB 
ID   A0A1G8P9F2_9RHOB        Unreviewed;       734 AA.
AC   A0A1G8P9F2;
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=SAMN05421850_106134 {ECO:0000313|EMBL:SDI89017.1};
OS   Lutimaribacter saemankumensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Lutimaribacter.
OX   NCBI_TaxID=490829 {ECO:0000313|EMBL:SDI89017.1, ECO:0000313|Proteomes:UP000199340};
RN   [1] {ECO:0000313|EMBL:SDI89017.1, ECO:0000313|Proteomes:UP000199340}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28010 {ECO:0000313|EMBL:SDI89017.1,
RC   ECO:0000313|Proteomes:UP000199340};
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};
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DR   EMBL; FNEB01000006; SDI89017.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8P9F2; -.
DR   STRING; 490829.SAMN05421850_106134; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000199340; 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; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199340}.
FT   DOMAIN          222..445
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          459..571
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          600..715
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          7..80
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         507
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         649
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   734 AA;  80333 MW;  74886D98537246E9 CRC64;
     MSLANKLAEE RRARLAAERL LELKQAELFA ANRKLGQHAR QLSEEIVETR AQVETYRDEN
     QRVKSDLTQA RQQVEIAERR LWLSIETIQD GFAFFDADNR MIAANNAYVG FFDGLEEVRP
     GTTYPRLLQL LTEEGIVNIG DMTPADWRAM MMARWQSPTP EPFVMRSYND QYIKLIDQRG
     HGGDVVSLAL NITATVRYES ELREARKVAE AANRAKSAFL ANMSHEIRTP MNGVVGMAEL
     LADTALSEEQ MLYVDTIRNS GEALLVIIND VLDYSKIEAE KLSLHPEPFD LERSIHELAM
     LLQPGAREKG LDILVDYDLF LPTVFMGDPG RVRQVLTNLM GNAVKFTTAG HVLVRVAGIA
     DEAGACHLHV TVEDTGIGIP EDKIEHVFGE FNQVESEQNR QFEGTGLGLA ISRRLIELMG
     GTIWVDSKEG EGTAFGFRIT LPLAEAQPDA PALPRDLRRV LIVDDLEVNR RILEKQMSAL
     GVSCSVCSTG AEALAALDDA IDLVMSDHNM PDMDGMELAA AIRETGSSVP IMILSSNPGV
     ADLDPARGMV QAVLPKPTPR AQLFARLQDM GMAPASADQA DGPDGSELVP AQTATARAMR
     ILAAEDNRTN QLVFRKMVQE LDIDLEFAAN GIEAVAAFSR FSPDIVFMDI SMPKMDGKAA
     TAEIRKQPGG DVPIVAMTAH AMEGDREAIL AAGLDGYLTK PLRKAAIWDM IGTYCPGGVR
     DPGTGTQPPQ AAAE
//
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