ID U5N9H7_9BURK Unreviewed; 1406 AA.
AC U5N9H7;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Cenrod_1891 {ECO:0000313|EMBL:AGX87970.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX87970.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX87970.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX87970.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
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: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP004885; AGX87970.1; -; Genomic_DNA.
DR RefSeq; WP_022774559.1; NC_022576.1.
DR STRING; 946483.Cenrod_1891; -.
DR KEGG; cbx:Cenrod_1891; -.
DR PATRIC; fig|946483.4.peg.1908; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2198; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_253957_0_0_4; -.
DR OrthoDB; 5290456at2; -.
DR Proteomes; UP000017184; Chromosome.
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; 3.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
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; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
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; 3.
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; PF08448; PAS_4; 2.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 3.
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; 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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AGX87970.1};
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:UP000017184};
KW Transferase {ECO:0000313|EMBL:AGX87970.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 218..263
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 298..354
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 355..425
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 439..493
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 494..539
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 582..634
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 652..873
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 892..1015
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1043..1160
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 201..228
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 605..645
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 946
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1093
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1406 AA; 153395 MW; 281100BD9AFD895A CRC64;
MNQYIHSSGS PESSALPLED RVAIEQVRLF CSQTHILFSI VLSVVVILAF FYGIAPLGHI
VGLGLFTVGV LVIRYQATLA VRKLAIHEFD IPAWKFRLIR LAVNSGGIYF LVGVIGYRYV
PHEYWGFLDL VVLASSGTAL GSMALVRGLF KFYVIPPATV AIVSHLLAGQ KYDYFMAAGM
MVTFLAYHSV SRYMGASVTE ALRLRIQNES LTEEAKQQNV KLAAILDNLP DATFVTDAQG
VVTAWNRAAE LMTGTMAKDI IGKGNYEYAV SFYGERRPVL IDLLLQMDDV TPHKYAHFSK
QGDTLSGEGY LPQRGLWFEA SASPLRDTSG TIYGGIEIVR DITARKNVML ELEQSKRRVD
DIINMLPDAA FVVDAEGMIT AWNRAAEMMT GAKAQDMIGK GHYEYAIAFY GQRRPIMIDA
VLHPDIDVRG HYHHFRKIGD VLAGEVSISP MGKELWIQAY ATALHDTQGQ VSGAIETIHD
ITGHKQLEDG LRASETKLST IIDFLPDATF VIDSEGIVTS WNRAAEQMTG IKAVDILGKG
NREYALAFYG ERKPILIDLV FMPDNDLLDA NYRHVQRFGE RIVAETAVNV RMGNQLWLQG
SASLLRDAEG NITGAIETIR DLTERKRMED DLAAARETAE RASQAKADFL ANMSHEIRTP
MNAIIGMSYL ALQTELNPKQ QHYVLKIHRA AENLLGIIND ILDFSKIEAG KLSLEQSPFQ
LYDVMDNLAN ILGIRVEDTG VELLFRISKN VPNALVGDAL RLSQVLVNLG NNAVKFTERG
EIIVGIETVS STSDTVQLHF WVQDTGIGMT QEQQGKLFQS FSQADASTTR KYGGTGLGLA
ISRNLIALMG GTIWADTTYG QGSTFHFHAQ FGLQDAPAFD RAIPLDTVQQ TRVLVVDDNA
TAREILSEMM LAWGMPTDVA AHGREALERL AYASQNGTPY GLVLMDWKMP GMDGIECLRH
LRTMELVSAP KVIIVTGHGK EEMQHAAQQQ GIDVHAVLIK PVTVSTLFDA IGEALSLHVP
SDRRAAARAK MHGQAMQSLR GARVLLVEDN EMNQELATEL LRKVGIDVVL ATNGQEALET
LARDDRFDGV LMDCQMPVMD GYTAAREIRK NPAWAALPII AMTANVITGE REKVLAVGMC
DHIGKPLNIE AMFDTLIHWI KPKQVVDASS PAGALPAPAA PAHFPALPGI NVNTGLAIAM
QDVRLYTSLL IRFREAMGQF ATLFGDARKH VAIHAGMDAG NHAMDSVDAA APERLAHTLK
GTAGNIGAAA VQAAAEELEL ACKNGEPPER IDALLQATLA ALHPVVVGLA SMGTGDAPAS
PLSDADAPPR DLAPVRNVVE QLGMLLAEGS IQAGEVLEAH ADLLQAAFPD HYHAMQEAIA
MFDFEVALHI LQAAQTAFSE KANISS
//
