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Database: UniProt
Entry: A0A1R1A957_9BACL
LinkDB: A0A1R1A957_9BACL
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ID   A0A1R1A957_9BACL        Unreviewed;      1302 AA.
AC   A0A1R1A957;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BK120_15550 {ECO:0000313|EMBL:OME82094.1};
OS   Paenibacillus sp. FSL A5-0031.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1920420 {ECO:0000313|EMBL:OME82094.1, ECO:0000313|Proteomes:UP000187447};
RN   [1] {ECO:0000313|EMBL:OME82094.1, ECO:0000313|Proteomes:UP000187447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL A5-0031 {ECO:0000313|EMBL:OME82094.1,
RC   ECO:0000313|Proteomes:UP000187447};
RA   Beno S.M.;
RT   "Paenibacillus species isolates.";
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}.
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:OME82094.1}.
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DR   EMBL; MRTD01000008; OME82094.1; -; Genomic_DNA.
DR   Proteomes; UP000187447; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   CDD; cd18773; PDC1_HK_sensor; 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; 6.10.340.10; -; 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; 4.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR036641; HPT_dom_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
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; 2.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF01627; Hpt; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
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; SSF158472; HAMP domain-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); 2.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50894; HPT; 1.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          315..368
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          366..437
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          455..507
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          504..542
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          576..628
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          646..868
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          887..1008
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1034..1150
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1199..1294
FT                   /note="HPt"
FT                   /evidence="ECO:0000259|PROSITE:PS50894"
FT   COILED          1270..1297
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         940
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1083
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1238
FT                   /note="Phosphohistidine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ   SEQUENCE   1302 AA;  147185 MW;  D68388F1D6A4CAF9 CRC64;
     MSKSGRFGSC VAEGGSGLKK MSLRTKGLIL IVLISFFPLL IAGIGNYSAV KDAMLKSEIE
     KTSSMQNKRA NELASWMAIR KAEVIVMSRT EVVRFGTDEE RLHYFGRELV RGGFIYHSIG
     YIDESGISLR TDGIRRDMSM ESFFQESITG KVVITDPFKP SFSDATQSFI VVPVYGATNE
     LKGVVYASIV MATLRPFIEF TGDQTIIRLF NDEGGIIYSS DNQEIISKGL FHEKSSLSPI
     AEKMLGSYEG VSEINIAGRS YAVFHTKVSE TPWRFALQEP MSKLEEEVKP IFWRIFTTIA
     VSEVIIVIFF FLYFERIVKR LERILGVTEQ AAAGSFEAEH LEVEPYDEIG QLGHSVNGMM
     EHLQEMFDRL EAIINQNQYA FIVLDDQYKV TYLNKTAEEM LGYKTSELAG SATPLLFMDL
     DEVRLEAEKL SEQLGRTVQP GLEVFKELRS TSFSYEREWT FIHKNGTRIP TLHSSNGLRD
     RNGRFSGVVG MVLDISDRKH VEKARNRLLD IVESAKDLIA SVSSRGKLVY MNGAGREMLG
     LQSNADQVHM VEEYSHPEMY SELVRGAALA KEFGYWESDA QLMKRNGEPL YVSMVIVPHK
     DEDTGELFFS CIARDISEQK MVQEKLVRAT LEAEEANQAK SRFLALMSHE IRTPLNGIIG
     LTQLMRKTGL SSSQKDYMDK MNTSSETLLR IINDILDFSK IEAGKVDIER QPFQPEELMH
     RITDQLSVFM GGKEQFEFII DTPEELPQTI IGDALRLEQV LLNLCMNAIK FTNRGKVRLK
     LEIVEQTDKG VNVKFIISDT GIGMSEAQVQ KLFKPFTQAD GSTTRKFGGT GLGLVISKSF
     VELMGGKLKV TSKALVGSEF YFTLPFTIIH KYTEPRLQVH QDLLEQPVWI VEDDDEMREH
     WSDIIESFGL TPIPFHSWKM ARDRLRRIGA GALPKLIVLD MEMPDMYGAE TWLEFHRDAE
     LAGVKTIAMT TSYGRDEMMQ LPAEQRPVTL LIKPIMRTAM LRAIESVLDH KGTDGKEQEI
     ESVATIQQNV TNTRILLAED NKINQLVAIE ILKERGYEVG LAENGEEVLI KLGEERWDLI
     LMDIHMPIMD GSEAVRIIRT QAKYDHIPII AVTANVLRND HERYLKLGMN DVVTKPISSE
     RIHNVISYWL KEINGSTIQP VVKSGLNDRS RALEPANIDS LPSIDGMDVE SALARVNGKL
     PILLHMMEQF MLDYDSFADQ LRMMVKQSEL TIVKRMAHTL KGAAGYLSAY ELLEAACEVE
     RIVKLPELES DNLQKAINQL EVTLKRLLDG LRKAKDVFDN KT
//
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