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Database: UniProt
Entry: Q7MGP9_VIBVY
LinkDB: Q7MGP9_VIBVY
Original site: Q7MGP9_VIBVY 
ID   Q7MGP9_VIBVY            Unreviewed;       427 AA.
AC   Q7MGP9;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=Transcription termination factor Rho {ECO:0000256|HAMAP-Rule:MF_01884};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01884};
DE   AltName: Full=ATP-dependent helicase Rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   Name=rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   OrderedLocusNames=VV3181 {ECO:0000313|EMBL:BAC95945.1};
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC95945.1, ECO:0000313|Proteomes:UP000002675};
RN   [1] {ECO:0000313|EMBL:BAC95945.1, ECO:0000313|Proteomes:UP000002675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016 {ECO:0000313|EMBL:BAC95945.1,
RC   ECO:0000313|Proteomes:UP000002675};
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA   Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA   Tsai S.F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Facilitates transcription termination by a mechanism that
CC       involves Rho binding to the nascent RNA, activation of Rho's RNA-
CC       dependent ATPase activity, and release of the mRNA from the DNA
CC       template. {ECO:0000256|HAMAP-Rule:MF_01884}.
CC   -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring
CC       structure. {ECO:0000256|HAMAP-Rule:MF_01884}.
CC   -!- SIMILARITY: Belongs to the Rho family. {ECO:0000256|HAMAP-
CC       Rule:MF_01884, ECO:0000256|PROSITE-ProRule:PRU01203}.
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DR   EMBL; BA000037; BAC95945.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7MGP9; -.
DR   STRING; 672.VV93_v1c29020; -.
DR   KEGG; vvy:VV3181; -.
DR   eggNOG; COG1158; Bacteria.
DR   HOGENOM; CLU_016377_4_3_6; -.
DR   Proteomes; UP000002675; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-UniRule.
DR   CDD; cd04459; Rho_CSD; 1.
DR   CDD; cd01128; rho_factor_C; 1.
DR   Gene3D; 1.10.720.10; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01884; Rho; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041703; Rho_factor_ATP-bd.
DR   InterPro; IPR011112; Rho_N.
DR   InterPro; IPR036269; Rho_N_sf.
DR   InterPro; IPR011113; Rho_RNA-bd.
DR   InterPro; IPR004665; Term_rho.
DR   NCBIfam; TIGR00767; rho; 1.
DR   PANTHER; PTHR46425; TRANSCRIPTION TERMINATION FACTOR RHO; 1.
DR   PANTHER; PTHR46425:SF1; TRANSCRIPTION TERMINATION FACTOR RHO; 1.
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   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF68912; Rho N-terminal domain-like; 1.
DR   PROSITE; PS51856; RHO_RNA_BD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01884};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01884};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW   ECO:0000256|HAMAP-Rule:MF_01884}.
FT   DOMAIN          56..131
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000259|PROSITE:PS51856"
FT   REGION          69..74
FT                   /note="RNA-binding 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   REGION          86..88
FT                   /note="RNA-binding 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   REGION          116..118
FT                   /note="RNA-binding 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   REGION          292..296
FT                   /note="RNA-binding 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         177..182
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         189..194
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   SITE            334
FT                   /note="RNA-binding 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ   SEQUENCE   427 AA;  47709 MW;  B078C0384532FD9F CRC64;
     MTKQESTTMN LTELKNKPVS DLVKLGESLG LENLARLRKQ DIIFAILKAH AKGGEDIFGD
     GVLEILQDGF GFLRSADSSY LAGPDDIYVS PSQIRRFNLR TGDSIAGKIR PPKDGERYFA
     LLKVNTVNDD RPDNARNKIL FENLTPLHAN ERMVMERGNG STEDITARVL DLASPIGKGQ
     RGLIVAPPKA GKTMLLQNIA QSITYNHPEC VLMVLLIDER PEEVTEMQRL VKGEVVASTF
     DEPASRHVQV AEMVIEKAKR LVEHKKDVVI LLDSITRLAR AYNTVVPSSG KVLTGGVDAN
     ALHRPKRFFG AARNVEEGGS LTIIATALVD TGSKMDEVIY EEFKGTGNME LHLNRKIAEK
     RVFPAIDFNR SGTRREELLT KPDELQKMWI LRKIVHPMGE TDAMEFLIDK LAMTKTNDEF
     FDAMRRQ
//
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