(data stored in ACNUC7421 zone)

SWISSPROT: C5B7P7_EDWI9

ID   C5B7P7_EDWI9            Unreviewed;       950 AA.
AC   C5B7P7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=RNA polymerase-associated protein RapA {ECO:0000256|HAMAP-Rule:MF_01821, ECO:0000256|SAAS:SAAS00632330};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01821, ECO:0000256|SAAS:SAAS00632350};
DE   AltName: Full=ATP-dependent helicase HepA {ECO:0000256|HAMAP-Rule:MF_01821};
GN   Name=rapA {ECO:0000256|HAMAP-Rule:MF_01821};
GN   OrderedLocusNames=NT01EI_0702 {ECO:0000313|EMBL:ACR67924.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67924.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transcription regulator that activates transcription by
CC       stimulating RNA polymerase (RNAP) recycling in case of stress
CC       conditions such as supercoiled DNA or high salt concentrations.
CC       Probably acts by releasing the RNAP, when it is trapped or
CC       immobilized on tightly supercoiled DNA. Does not activate
CC       transcription on linear DNA. Probably not involved in DNA repair.
CC       {ECO:0000256|HAMAP-Rule:MF_01821, ECO:0000256|SAAS:SAAS00632342}.
CC   -!- SUBUNIT: Interacts with the RNAP. Has a higher affinity for the
CC       core RNAP than for the holoenzyme. Its ATPase activity is
CC       stimulated by binding to RNAP. {ECO:0000256|HAMAP-Rule:MF_01821,
CC       ECO:0000256|SAAS:SAAS00632325}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01821,
CC       ECO:0000256|SAAS:SAAS00632347}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001600; ACR67924.1; -; Genomic_DNA.
DR   STRING; 634503.NT01EI_0702; -.
DR   EnsemblBacteria; ACR67924; ACR67924; NT01EI_0702.
DR   KEGG; eic:NT01EI_0702; -.
DR   eggNOG; ENOG4105BZK; Bacteria.
DR   eggNOG; COG0553; LUCA.
DR   HOGENOM; HOG000218482; -.
DR   KO; K03580; -.
DR   OMA; MSILERD; -.
DR   OrthoDB; POG091H02YR; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   HAMAP; MF_01821; Helicase_RapA; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR023949; Helicase_RapA.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR022737; RapA_C.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF808; PTHR10799:SF808; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF12137; RapA_C; 1.
DR   Pfam; PF00176; SNF2_N; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B7P7.
DR   SWISS-2DPAGE; C5B7P7.
KW   Activator {ECO:0000256|HAMAP-Rule:MF_01821,
KW   ECO:0000256|SAAS:SAAS00632328};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01821,
KW   ECO:0000256|SAAS:SAAS00632337};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_01821,
KW   ECO:0000256|SAAS:SAAS00632336};
KW   Helicase {ECO:0000256|HAMAP-Rule:MF_01821,
KW   ECO:0000256|SAAS:SAAS00632343};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01821,
KW   ECO:0000256|SAAS:SAAS00632332};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01821,
KW   ECO:0000256|SAAS:SAAS00632341};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_01821,
KW   ECO:0000256|SAAS:SAAS00632349};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01821,
KW   ECO:0000256|SAAS:SAAS00632345}.
FT   DOMAIN      146    316       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      472    646       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   NP_BIND     159    166       ATP. {ECO:0000256|HAMAP-Rule:MF_01821}.
FT   MOTIF       262    265       DEAH box. {ECO:0000256|HAMAP-Rule:
FT                                MF_01821}.
SQ   SEQUENCE   950 AA;  107411 MW;  C786B5D5CDE16062 CRC64;
     MGTVVALDAR MVTLLFPATG ENRLYARNDS PITRVMFNPG DTITTHEGWQ LCVEEVQEHE
     GLLTYIGNRC DNGENSVAVR EVLLDSRLTF SKPQDRLFAG QIDRMDRFAL RYRARKYQSE
     QFRLPCSGLR GMRASLIPHQ LHIARDVGQR HAPRVLLADE VGLGKTIEAG MIIHQQLLSG
     RAERVLIVVP ETLQHQWLVE MLRRFNLRVA LFDDERYAEA AQDSSNPFET EQLVICSLDF
     VRRSRQRLEQ LADASWDLLV VDEAHHLAWS EQAPSREYQV IEQLAEQIPG VLLLTATPEQ
     LGQESHFARL RLLDPNRFHD YAQFVAEQLR YRPVADAVTL LLNDGHLQQD ELNMLCEMVA
     EQDIEPLLKA ANTDGEDSQQ ARAELVRMLM DRHGTSRVLF RNTRQGVKGF PQRTLHQITL
     PLPAQYQTAI KVSGIMGSKK SVEAQANDML YPERIYQEFE GENATWWNFD PRAEWLLDFL
     LTQRDEKVLV ICAQAATAIH LEQLLREREG IRAAVFHQGM SLIERDRAAA YFASQEEGAQ
     VLLCSEIGSE GRNFQFANHL VMFDLPFNPD LLEQRIGRLD RIGQARDIQI YVPCLEGTAQ
     SVLIRWYHQG LDAFEHTCPT GRTIYDRYYE TLLAFLAKPA QLDGFDDFIK TCRTDHDTLK
     IQLEKGRDRL LEMHSNGGEA AQALAGSIAA QDNDVNLVNF ALNLFDIVGI NQEDRSDSLI
     VLTPSDHMLV PDFPGLPQDG CTVTFDREQA LSREDAQFIS WEHPLMRNGL DLILSGDTGS
     SAVSLLKNKA LPVGTLLLEA VYVVEAQAPK QLQLTRFLPP TPVRMLLDAK GNDLAAQVEF
     ESFNRQLNAV NRHTASKLVN AVQPNVHAML QSGEALIADQ AQALIDAAKR EADEALSAEL
     ARLESLRAVN PNIRDDELET LEFTRRKVLE TLDQAGWRLD ALRLIVVSHQ
//

If you have problems or comments...

PBIL Back to PBIL home page