ID W8FAY0_9BACT Unreviewed; 742 AA.
AC W8FAY0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 50.
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 ORFNames=Hsw_3260 {ECO:0000313|EMBL:AHJ98855.1};
OS Hymenobacter swuensis DY53.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1227739 {ECO:0000313|EMBL:AHJ98855.1, ECO:0000313|Proteomes:UP000019423};
RN [1] {ECO:0000313|EMBL:AHJ98855.1, ECO:0000313|Proteomes:UP000019423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY53 {ECO:0000313|EMBL:AHJ98855.1,
RC ECO:0000313|Proteomes:UP000019423};
RA Jung J.-H., Jeong S.-W., Joe M.-H., Cho y.-j., Kim M.-K., Lim S.-Y.;
RT "Complete genome sequence of ionizing-radiation resistance bacterium
RT Hymenobacter swuensis DY53.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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; CP007145; AHJ98855.1; -; Genomic_DNA.
DR RefSeq; WP_044002975.1; NZ_CP007145.1.
DR AlphaFoldDB; W8FAY0; -.
DR STRING; 1227739.Hsw_3260; -.
DR KEGG; hsw:Hsw_3260; -.
DR PATRIC; fig|1227739.3.peg.3427; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_1_2_10; -.
DR OrthoDB; 9805197at2; -.
DR Proteomes; UP000019423; Chromosome.
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:UP000019423};
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 374..450
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000259|PROSITE:PS51856"
FT REGION 48..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 493..498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 505..510
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 536
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ SEQUENCE 742 AA; 81495 MW; D652CDAFFB5C0D30 CRC64;
MYTIDELKDR LLSELKEVAE TLKVGNFKKL SKQDLIYKIL DQQAITPTDK LPQKVKSGEV
AAPAVSAAPY TEPVEAAAAK TPAVKAAPAA KTTGTRAARP AAARPARGKA AAAPAEVTTS
ETEAAPVAIA GPVAPDAPVV ATEPTPVAAE VVVAEPTGTA PAEAAPAEDT ASIERPVKLY
QRPERRTRTD RAGRPIVAGA EATATEEEAA PAAETVVETP VAPMRDPRPI DPTAPAPLRE
GRPEQPRIFR DGREYIPREA RTDAARAEIR PDSSSRSEQP RDLRNDQPRT DGRQEGALRD
GSRPEQPRNL REGGRPDARD QREQRREERY AARELQRQQR QEQRLTERQN GTAEQPTRVE
RAEQRPARQD FDITIPGDGT LEMMPDGGYG FLRSPFYNYL ASPDDIYVAP QQVKQFGLKA
GDTVKCTIRP PRDGEKYFAL VGVDGINGRS VEDARDRIPF SNLTPLFAEE RLKLTTKSAQ
YSTRIMDLFA PIGKGQRGLI VAQPKTGKTV LLQEIANAIS ENHPEVYLMI LLIDERPEEV
TDMARSVKAE VLSSTFDETA DRHVKIATIA MEKAKRLVEC GHDVVILLDS ITRLARAYNT
VQPASGKILS GGVDANALHK PKRFFGAARN VENGGSLTIV ATALIETGSK MDEVIFEEFK
GTGNMELQLD RKLANKRIFP AIDVPASGTR REDLLMSKDE LNRIWVLRKF MSDMTAAEAM
EFLKDRMKGT RDNNEFLLAM NG
//
