ID I3CEF2_9GAMM Unreviewed; 1322 AA.
AC I3CEF2;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BegalDRAFT_1092 {ECO:0000313|EMBL:EIJ41995.1};
OS Beggiatoa alba B18LD.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Thiotrichaceae; Beggiatoa.
OX NCBI_TaxID=395493 {ECO:0000313|EMBL:EIJ41995.1, ECO:0000313|Proteomes:UP000005744};
RN [1] {ECO:0000313|EMBL:EIJ41995.1, ECO:0000313|Proteomes:UP000005744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B18LD {ECO:0000313|EMBL:EIJ41995.1,
RC ECO:0000313|Proteomes:UP000005744};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Held B., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Samuel K., Teske A.,
RA Mueller J., Woyke T.;
RT "Improved High-Quality Draft sequence of Beggiatoa alba B18lD.";
RL Submitted (NOV-2011) 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}.
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DR EMBL; JH600070; EIJ41995.1; -; Genomic_DNA.
DR STRING; 395493.BegalDRAFT_1092; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3706; Bacteria.
DR HOGENOM; CLU_259744_0_0_6; -.
DR OrthoDB; 6724607at2; -.
DR Proteomes; UP000005744; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; cd01949; GGDEF; 1.
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; cd12913; PDC1_MCP_like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 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; 3.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR000160; GGDEF_dom.
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; IPR029787; Nucleotide_cyclase.
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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43047:SF83; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00267; GGDEF; 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; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000005744};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 352..375
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 373..425
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 447..665
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 704..821
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 840..876
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 917..971
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 979..1044
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1183..1320
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT COILED 410..447
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1128..1155
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 754
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1322 AA; 150238 MW; 053F969BEED24199 CRC64;
MSYYWRAWLV RFTKRIPLRV MLTIPFISLI VIVVSLTSGL PLYYGHQVVN NIAEELRHEV
TNRIQENIQN YLATAHLVNQ VNANALINSL NQENTQDLSQ LENFFVKQIH TFPSISYSYF
ATPDNQLIGA GQNASGEQFI LQGHAKERAL QFYAINAEGT RGKFQRQIED YLPTERPWFK
VAREHSRPVW SEVFISLGEQ ELAITAVQGV YDKQQQLQGI FGTSLLFSGI HQFLHKFKLG
DFGQLFIIDR SGQLIATSNE SPTFYKQDGH YTRLNLDSTL DPLIHSAGQN ILTQLHSFKD
IWMEKNLTFD FENRSYLAQV TPLNDQWGLD WLIVIVIPQS DFTEHLTEKN QITLSVSLFI
FCLAVIIGIW LAHWIGQPIF NLHIAVQRFM QGEWHYPIRV THTKELNQLA QAFRRLAKQL
NATIKRLADK NAELKRLDQL KDEFLANTSH ELRTPLNGII GLAESLLDNT EQTLNPHIQQ
NLSMIAMSGR RLANLVNDLL DFSKLKHKDL QLQLKPISVR EAVDIACQLN APLVKQQHLT
LYNQIATDLP LILADENRLQ QILNNLLSNA IKFTPQGSIS ITATLAPPMV QIHIQDTGIG
IAPEDIARIF ESFEQADGQT ARTYGGTGLG LAITKQLVEL HGGQISVTSI QEQGSCFTVS
LPIASNMSQV LTPLTYCPVR YEPNLLSEVL QIARVYPNQH TLGKILLVDD ELINLHVLSN
YLTPHGYELI HATSGHEVLQ ILEDGVKPDL ILLDIMMPKM TGYEVCKKVR ARYNANELPI
IIISAKNQVN DLVSGLNAGA NDYLVKPVWK DELLARMRIH LQLAEVSIEN MRLCAELSDN
EHRLTQILES LPVGLLVTDH QGKVIYINRM GQMITGQDVS SGVNVQTLSK SYHYYLAGTN
QLYPTEELLL AKALAGETCT IDNIEILRND KRIPLESWGT PVFDEKHQVR YAIAVFQDIS
KRRQAEQERT HYLQALQASE ERFRLIMEML PIPLVINEIE SGRILFANSQ VHTVYGVAVN
QLLGRSTLDL YADPSERQTV IEQFLAQNGQ LRHKEVRHKR LDNQTILWVS LFLQRMEYNG
QQTIITVLLD ITAQKKAQEE RVRLIRAIEA EKAVLSMNYK LQQEIYQRQQ TEIALQKAYA
DLEKANADLQ QLATHDQLTQ LANRYWFDEY YAQTWKQMCR EQKQLSLIMA DVDFFKNYND
KYGHLQGNDC LQQVAAALMN SIKRPADLVA RYGGEEFAII LPNTDEAGAL HVAQRIQANL
QEKAIVHEYS HVAKHITLSI GIATLIPHAN IPLDRLVAIA DQALYEAKDA GRNRIASKTV
ML
//
