ID   D2RCV0_GARV4            Unreviewed;       656 AA.
AC   D2RCV0;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   31-MAY-2011, entry version 13.
DE   RecName: Full=Transcription termination factor Rho;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase Rho;
GN   Name=rho; OrderedLocusNames=HMPREF0424_0110;
OS   Gardnerella vaginalis (strain 409-05).
OC   Bacteria; Actinobacteria; Actinobacteridae; Bifidobacteriales;
OC   Bifidobacteriaceae; Gardnerella.
OX   NCBI_TaxID=553190;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=20865041; DOI=10.1371/journal.pone.0012411;
RA   Yeoman C.J., Yildirim S., Thomas S.M., Durkin A.S., Torralba M.,
RA   Sutton G., Buhay C.J., Ding Y., Dugan-Rocha S.P., Muzny D.M., Qin X.,
RA   Gibbs R.A., Leigh S.R., Stumpf R., White B.A., Highlander S.K.,
RA   Nelson K.E., Wilson B.A.;
RT   "Comparative genomics of Gardnerella vaginalis strains reveals
RT   substantial differences in metabolic and virulence potential.";
RL   PLoS ONE 5:e12411-e12411(2010).
CC   -!- FUNCTION: Facilitates transcription termination by a mechanism
CC       that involves Rho binding to the nascent RNA, activation of Rho's
CC       RNA-dependent ATPase activity, and release of the mRNA from the
CC       DNA template (By similarity).
CC   -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring
CC       structure (By similarity).
CC   -!- SIMILARITY: Belongs to the Rho family.
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DR   EMBL; CP001849; ADB13452.1; -; Genomic_DNA.
DR   RefSeq; YP_003373377.1; NC_013721.1.
DR   GeneID; 8709503; -.
DR   GenomeReviews; CP001849_GR; HMPREF0424_0110.
DR   KEGG; gva:HMPREF0424_0110; -.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004386; F:helicase activity; IEA:HAMAP.
DR   GO; GO:0003723; F:RNA binding; IEA:HAMAP.
DR   GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:InterPro.
DR   GO; GO:0003715; F:transcription termination factor activity; IEA:HAMAP.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   HAMAP; MF_01884; Rho; 1; -.
DR   InterPro; IPR000194; ATPase_a/bsu_nucl-bd.
DR   InterPro; IPR003593; ATPase_AAA+_core.
DR   InterPro; IPR011129; Cold_shock_prot.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR011112; Rho_N.
DR   InterPro; IPR011113; Rho_RNA-bd.
DR   InterPro; IPR004665; Term_rho.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 2.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF07498; Rho_N; 1.
DR   Pfam; PF07497; Rho_RNA_bind; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00959; Rho_N; 1.
DR   TIGRFAMs; TIGR00767; Rho; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Complete proteome; Helicase; Hydrolase;
KW   Nucleotide-binding; RNA-binding; Transcription;
KW   Transcription regulation; Transcription termination.
FT   NP_BIND     392    397       ATP (By similarity).
FT   NP_BIND     404    409       ATP (By similarity).
FT   BINDING     435    435       ATP (By similarity).
SQ   SEQUENCE   656 AA;  73981 MW;  508B517B294E6959 CRC64;
     MATGQNLEKM KLSELKDLAK QMGLRGTSTM RKPELVATLT AARNGGEAPA GVSVRVPRDV
     VNANKTADTS TDIEDVRSSK DNSDLEALEV LVPNAASDRR YRDEEDFGNK NYRRDANRNN
     TFQRRRSSED RNDNRDRRED GMDSHELDQI LATLPGEDSH AEGEQRRQRV ASRDFDREEQ
     QNRADRFQRR MRGRARDYDE SRSDYSDRQN RSERMDRVER DDRDERRAER GERQDRNDRN
     VRLDRDARDA RDSREEHDLR EIRREEPQEE LVPVAGIVDV LESYAFVRTS GYLPGPNDVY
     VSMSQIKKYG LRKGDAVQGS IRAPREGDRR NQRQKFVPLQ TVNSINGMSV EEAQSRPQFA
     KLTPLYPQER LKQETTPNRM LGRVIDLVAP IGKGQRGLIV SPPKAGKTIT LQNIANAITT
     NNPEVHLMVV LVDERPEEVT DMERTVQGEV ISSTFDRPAT DHTTVAELAI ERAKRLVELG
     QDVVVLLDSM TRLARAYNIA APTSGRILSG GVDAQALYPP KKFFGAARNI EDGGSLTIIS
     SALVETGSKM DEVIFEEFKG TGNMELRLSR DLADKRLFPA VDINASGTRR EELITPAADL
     PVIYRLRRLF GGLEAEQAYQ TLIPRLKKTA SNRDFLAAIT QQTGTATNNS SSTTIA
//