ID A0A174RGR6_9BACE Unreviewed; 732 AA.
AC A0A174RGR6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 43.
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 ECO:0000313|EMBL:CUP84624.1};
GN ORFNames=DWY26_01320 {ECO:0000313|EMBL:RGR74455.1}, DXA49_20220
GN {ECO:0000313|EMBL:RGY21993.1}, ERS852494_02197
GN {ECO:0000313|EMBL:CUP41128.1}, ERS852558_01142
GN {ECO:0000313|EMBL:CUP84624.1}, F2Y31_15250
GN {ECO:0000313|EMBL:KAA5496967.1}, F2Y35_18695
GN {ECO:0000313|EMBL:KAA5488226.1}, F2Y36_11680
GN {ECO:0000313|EMBL:KAA5463083.1}, F2Y39_07870
GN {ECO:0000313|EMBL:KAA5478873.1};
OS Bacteroides caccae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=47678 {ECO:0000313|EMBL:CUP84624.1, ECO:0000313|Proteomes:UP000095725};
RN [1] {ECO:0000313|Proteomes:UP000095657, ECO:0000313|Proteomes:UP000095725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834880 {ECO:0000313|EMBL:CUP41128.1,
RC ECO:0000313|Proteomes:UP000095657}, and 2789STDY5834946
RC {ECO:0000313|EMBL:CUP84624.1, ECO:0000313|Proteomes:UP000095725};
RG Pathogen Informatics;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000284205, ECO:0000313|Proteomes:UP000284431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF24-29LB {ECO:0000313|EMBL:RGR74455.1,
RC ECO:0000313|Proteomes:UP000284205}, and OF02-6LB
RC {ECO:0000313|EMBL:RGY21993.1, ECO:0000313|Proteomes:UP000284431};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000368418, ECO:0000313|Proteomes:UP000427825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BIOML-A19 {ECO:0000313|EMBL:KAA5496967.1,
RC ECO:0000313|Proteomes:UP000368418}, BIOML-A21
RC {ECO:0000313|EMBL:KAA5488226.1, ECO:0000313|Proteomes:UP000491168},
RC BIOML-A25 {ECO:0000313|EMBL:KAA5478873.1,
RC ECO:0000313|Proteomes:UP000427825}, and BIOML-A31
RC {ECO:0000313|EMBL:KAA5463083.1, ECO:0000313|Proteomes:UP000475905};
RX PubMed=31477907; DOI=.1038/s41591-019-0559-3;
RA Poyet M., Groussin M., Gibbons S.M., Avila-Pacheco J., Jiang X.,
RA Kearney S.M., Perrotta A.R., Berdy B., Zhao S., Lieberman T.D.,
RA Swanson P.K., Smith M., Roesemann S., Alexander J.E., Rich S.A., Livny J.,
RA Vlamakis H., Clish C., Bullock K., Deik A., Scott J., Pierce K.A.,
RA Xavier R.J., Alm E.J.;
RT "A library of human gut bacterial isolates paired with longitudinal
RT multiomics data enables mechanistic microbiome research.";
RL Nat. Med. 25:1442-1452(2019).
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01884}.
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DR EMBL; CZAI01000004; CUP41128.1; -; Genomic_DNA.
DR EMBL; CZBL01000003; CUP84624.1; -; Genomic_DNA.
DR EMBL; VVYP01000013; KAA5463083.1; -; Genomic_DNA.
DR EMBL; VVYJ01000003; KAA5478873.1; -; Genomic_DNA.
DR EMBL; VVYF01000021; KAA5488226.1; -; Genomic_DNA.
DR EMBL; VVYD01000015; KAA5496967.1; -; Genomic_DNA.
DR EMBL; QRUO01000001; RGR74455.1; -; Genomic_DNA.
DR EMBL; QSCS01000044; RGY21993.1; -; Genomic_DNA.
DR RefSeq; WP_005681576.1; NZ_VVYQ01000012.1.
DR STRING; 47678.ERS852494_02197; -.
DR GeneID; 75115298; -.
DR KEGG; bcac:CGC64_16245; -.
DR Proteomes; UP000095657; Unassembled WGS sequence.
DR Proteomes; UP000095725; Unassembled WGS sequence.
DR Proteomes; UP000284205; Unassembled WGS sequence.
DR Proteomes; UP000284431; Unassembled WGS sequence.
DR Proteomes; UP000368418; Unassembled WGS sequence.
DR Proteomes; UP000427825; Unassembled WGS sequence.
DR Proteomes; UP000475905; Unassembled WGS sequence.
DR Proteomes; UP000491168; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000095657};
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 363..438
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000259|PROSITE:PS51856"
FT REGION 55..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 483..488
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 495..500
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 526
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ SEQUENCE 732 AA; 81684 MW; 7CD6754680551E90 CRC64;
MYNIIQLNDK DLSELQVIAK ELGIKKTDSL KKEDLVYKIL DEQAIAGATK KVAADKLKEE
RKEEQKKKRS RVAPAKKDNK VVSATKEGEA EKAKEAAPAK PQQPSKKEES ANKEKETPAV
EVKAENTAAP KRKVGRPRKN ADAAEQKEVE SVKTATPATP KVTEDKVVTE KAPEVIEKAV
PAQAPEKKTK ANKPAEEKKV VVKPQPQKKA EPVIDEESNI LSGADDDDFI PIEDLPSEKI
ELPTELFGKF EATKTEPAQT ATEQQAPQPQ QQAHQQQQQQ RPRIVRPRDN NNGNNNASNS
NNNANNNNNN NFQRNNNQNQ NQQRVPMPRP AQPNNANENL PVPQQQQERK VIEREKPYEF
DDILNGVGVL EIMQDGYGFL RSSDYNYLSS PDDIYVSQSQ IKLFGLKTGD VVEGVIRPPK
EGEKYFPLVK VSKINGRDAA FVRDRVPFEH LTPLFPDEKF KLCKGGYSDS MSARVVDLFA
PIGKGQRALI VAQPKTGKTI LMKDIANAIA ANHPEVYMIM LLIDERPEEV TDMARSVNAE
VIASTFDEPA ERHVKIAGIV LEKAKRLVEC GHDVVIFLDS ITRLARAYNT VSPASGKVLS
GGVDANALHK PKRFFGAARN IENGGSLTII ATALIDTGSK MDEVIFEEFK GTGNMELQLD
RNLSNKRIFP AVNITASSTR RDDLLLDKTT LDRMWILRKY LADMNPIEAM DFVKDRLEKT
RDNDEFLMSM NS
//
