(data stored in SCRATCH zone)

SWISSPROT: C3MGL8_SINFN

ID   C3MGL8_SINFN            Unreviewed;      1117 AA.
AC   C3MGL8;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   SubName: Full=Predicted sensor histidine kinase protein with ATP-binding domain {ECO:0000313|EMBL:ACP24133.1};
GN   OrderedLocusNames=NGR_c03350 {ECO:0000313|EMBL:ACP24133.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24133.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24133.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
CC       phospho-L-histidine. {ECO:0000256|SAAS:SAAS00414205}.
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DR   EMBL; CP001389; ACP24133.1; -; Genomic_DNA.
DR   RefSeq; WP_012706918.1; NC_012587.1.
DR   RefSeq; YP_002824886.1; NC_012587.1.
DR   ProteinModelPortal; C3MGL8; -.
DR   STRING; 394.NGR_c03350; -.
DR   EnsemblBacteria; ACP24133; ACP24133; NGR_c03350.
DR   GeneID; 7791561; -.
DR   KEGG; rhi:NGR_c03350; -.
DR   PATRIC; fig|394.7.peg.3140; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; ENOG410XNMH; LUCA.
DR   HOGENOM; HOG000271352; -.
DR   OMA; HKTDFLA; -.
DR   OrthoDB; POG091H03T5; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
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 transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   4: Predicted;
DR   PRODOM; C3MGL8.
DR   SWISS-2DPAGE; C3MGL8.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00776324,
KW   ECO:0000313|EMBL:ACP24133.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Kinase {ECO:0000256|SAAS:SAAS00494113, ECO:0000313|EMBL:ACP24133.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00777800};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Transferase {ECO:0000256|SAAS:SAAS00494184}.
FT   DOMAIN      749    819       PAS (PER-ARNT-SIM). {ECO:0000259|PROSITE:
FT                                PS50112}.
FT   DOMAIN      892   1113       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
SQ   SEQUENCE   1117 AA;  118451 MW;  A6C8146143186B11 CRC64;
     MPARQYPFID IAVHARVREH FARGDAAVLF SKDLARVLWA NDQGARLFGV ASVYDFIDGA
     LSATDLSLRQ LRAAAEQLAA VGDRRQLLIR IAAGFRRLPL NATVEMIRIR PGEEAVLFTA
     PHNGKALSAE ERAAAMIAGL DGPDTHMAVL DDDGEIVARS PGFEHLGLSG DIRRTLVSAV
     AREKDRLIKR LVATEKGQLP AAIGKISDHP ALHLLFAVET TLDTPDAEEA AAKDEPDAIA
     AAAAEVGTGL PSPTTLDEPA ETPLREDTSE AEATTDPAAT DEPTDAPSLG EEHGELALRS
     GDEAADLAPS AEAAEPAPEV ATSDADSAAA AASGFTFTPG SRAVRFVWKI DAEGCFSEIS
     EEFAAAVGPK SADVVGLTFS ELAARYDLDP DNKVNALLHR RDTWSGKTIL WPIEGTSLKV
     PVDLAALPTY SRSREFDGFR GFGIVRIADA VEDEKASGLS LGHIDTPRNE GMPAEAPSDD
     APREPASLAS DGTDTPRSEA EPPSAEDPFA GERPALRIVD IPARPPSDKV IDLDEHRPGS
     SGTLTRGEQA AFREIARQLG AQFSETTPPA AADEDGKRPV DAASQAEAAG DMESLSSEDA
     TAARQEETMP GAGDEAPPAP RGGVGMSSEI LDRLPVALLI HHGDELLHAN PEFLRLTGYR
     KLEAFQQAGG LEALFAYGAE SGEHEPDGTM TLVRANGPLA PVSAHLHSIQ WEGRSALMLA
     LAPAAARAAD MPSAGADASA GGEARLRMEI DELRSILETA TDGVVVLGQD GDIRTMNGSA
     SALFNYDEDE MRGKPFAALF AHESQKAVID YLQGLSGHGV ASVLNDGREA IGREAGGGFL
     PLFMTIGRLS SSNGYCAVIR DITQWKRTEE ELRNAKRSAE TANAHKTEFL ARVSHEIRTP
     LNAIIGFSDM MASEHFGPIG NPRYIEYAGD IGRSGRHVLD IVNDLLDISK IEAGEMELDF
     SAVDLNEAVS EAVSLVQPQA NSQRVIIRTS LSGSVPEVVA DGRSIKQIAL NILANAIRFT
     PSGGQIVVST SYETNGSVIL RIRDTGIGMT RNELDQAMKP FRQVTTGGRK RGEGTGLGLP
     LTKAMAEANR AQFGISSAPN EGTLVEISFP SQRVLAN
//

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