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Database: UniProt
Entry: A0A0B3S8P4_9RHOB
LinkDB: A0A0B3S8P4_9RHOB
Original site: A0A0B3S8P4_9RHOB 
ID   A0A0B3S8P4_9RHOB        Unreviewed;       881 AA.
AC   A0A0B3S8P4;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=OA50_00369 {ECO:0000313|EMBL:KHQ55333.1};
OS   Mameliella alba.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Mameliella.
OX   NCBI_TaxID=561184 {ECO:0000313|EMBL:KHQ55333.1, ECO:0000313|Proteomes:UP000030960};
RN   [1] {ECO:0000313|EMBL:KHQ55333.1, ECO:0000313|Proteomes:UP000030960}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMTAT08 {ECO:0000313|EMBL:KHQ55333.1,
RC   ECO:0000313|Proteomes:UP000030960};
RA   Gan H.Y., Muhd D.-D., Mohd Noor M.E., Yeong Y.S., Usup G.;
RT   "Genome sequence of Ponticoccus sp. strain UMTAT08 isolated from clonal
RT   culture of toxic dinoflagellate Alexandrium tamiyavanichii.";
RL   Submitted (OCT-2014) 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: 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:KHQ55333.1}.
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DR   EMBL; JSUQ01000001; KHQ55333.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0B3S8P4; -.
DR   STRING; 561184.SAMN05216376_103372; -.
DR   OrthoDB; 9801651at2; -.
DR   Proteomes; UP000030960; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 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; 1.20.120.160; HPT 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; IPR036641; HPT_dom_sf.
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   InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
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; PF01627; Hpt; 1.
DR   Pfam; PF00989; PAS; 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; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 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; PS50894; HPT; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:KHQ55333.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000030960};
KW   Transferase {ECO:0000313|EMBL:KHQ55333.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        203..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          238..292
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          385..603
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          625..742
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          778..877
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         674
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         819
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   881 AA;  96642 MW;  DD7F8640E6F065B0 CRC64;
     MQSPALVLGR QHRVNQGPER TPGRDGPGWM SSLPNWLTGI VIVMIVVSIA VLVLDLQQQT
     RRLASSAADN MQWTLGQAEV ELMALEISAL RADTGDVSLS DVRLRYDIFY SRVETLTESH
     RFETLMQIGV MPERIEEIRT FRSNWLPLID GPDEALRAAL PDLAEDARSV RTTVRDTTLA
     GVEFFSQQGF EQRDSLSRSM VRVGLLTVAL VILLAVLALM LFRLARKSDA EARANRETRE
     RIETILSTSL DAVVVSDAAG RILDYNGAAE RIFGYDRNQA LGADMADLIV PDHYRAAHRR
     GMARFRRDGD ARVIGKGIVR LDARRSDGTV FPVDLSLARA QSPAGEIYIA FLRDISDRVR
     NEAELKRARD RAIAGEKQKA ELLAVMSHEM RTPLNGMLGT LELVDDQSLD ARHQRYLRIV
     RDSGRILLGH VNDVLDISRL DAGKMTLRKS GFDLVRLLED IVDNQGQHAS ARGNRLILVP
     PNPELHRVYG DPDRLRQILL NLVGNAIKFT WNGRITLEAD CAAGLESVEL RVTDTGIGIA
     EEDIDRIFED FVTIDSTYGR STSGTGLGLG ISLRLATVLG GELGVESEPG DGSVFWLRVP
     LAPPEEKPMP EVPSPEPCER PPACDVLLVE DNEINRLVGR DLLERDGHRV ETANSGEAAL
     SALGTRRFDV VMMDISMPGM DGIDVARALR HSAGINAATP VVATTAHALP QEVEAFHAAG
     MQAVLIKPLT LDAIRTVLTE VLAAGAAVRP VATRPPAPGD QTTVIDEAHL EEMRQDLAPA
     RLRHLHERFL FEMTDFQHAM PDLAKAGITG QATLAAEAHR MAGSAAMMGA ARLMALLQEI
     EQAAKAGNAM ELDARQADLA ECWQTTRDAL SAVLRPVEQL H
//
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