ID H8N0U7_CORCM Unreviewed; 530 AA.
AC H8N0U7;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
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 Synonyms=rho1 {ECO:0000313|EMBL:AFE10133.1};
GN OrderedLocusNames=COCOR_05602 {ECO:0000313|EMBL:AFE10133.1};
OS Corallococcus coralloides (strain ATCC 25202 / DSM 2259 / NBRC 100086 / M2)
OS (Myxococcus coralloides).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Corallococcus.
OX NCBI_TaxID=1144275 {ECO:0000313|EMBL:AFE10133.1, ECO:0000313|Proteomes:UP000007587};
RN [1] {ECO:0000313|EMBL:AFE10133.1, ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RX PubMed=22582372; DOI=10.1128/JB.00397-12;
RA Huntley S., Zhang Y., Treuner-Lange A., Kneip S., Sensen C.W.,
RA Sogaard-Andersen L.;
RT "Complete Genome Sequence of the Fruiting Myxobacterium Corallococcus
RT coralloides DSM 2259.";
RL J. Bacteriol. 194:3012-3013(2012).
RN [2] {ECO:0000313|Proteomes:UP000007587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25202 / DSM 2259 / NBRC 100086 / M2
RC {ECO:0000313|Proteomes:UP000007587};
RA Huntley S., Zhang Y., Treuner-Lange A., Sensen C.W., Sogaard-Andersen L.;
RT "Genome sequence of the fruiting myxobacterium Corallococcus coralloides
RT DSM 2259.";
RL Submitted (MAR-2012) 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; CP003389; AFE10133.1; -; Genomic_DNA.
DR AlphaFoldDB; H8N0U7; -.
DR STRING; 1144275.COCOR_05602; -.
DR KEGG; ccx:COCOR_05602; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_0_7; -.
DR InParanoid; H8N0U7; -.
DR OrthoDB; 9805197at2; -.
DR Proteomes; UP000007587; 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; cd01128; rho_factor_C; 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; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR041703; Rho_factor_ATP-bd.
DR InterPro; IPR011113; Rho_RNA-bd.
DR InterPro; IPR004665; Term_rho.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51856; RHO_RNA_BD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_01884};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01884};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01884};
KW Reference proteome {ECO:0000313|Proteomes:UP000007587};
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 167..240
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000259|PROSITE:PS51856"
FT REGION 1..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 283..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 295..300
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 326
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ SEQUENCE 530 AA; 58597 MW; 4BEB9B093D298D7D CRC64;
MSENSDNPET RNPPPPPAAA RPPPPPEADD DGGDDEGDEG PDEGEASAGG AAQNGAPGAP
GQGGRRRRRR RRRRGAQVHF TPEGQAYRMT AGPDGQQVQV FLTPQELEQY RQRQAQQQQQ
QPQGGGQPQG QENRPQDGGQ PQPRHEHPRH QQQQRGGHAQ GAPQQNLAPV EGVLDTEAKG
PNAFLRQVKR NLLASPDDPE LPKNLVQKLR LRQGQYLTAF AQMRGHKGVI QKVDTVDGRP
LDGAPRLPHF ADLTSVDPTE RLKLENGHKE MVTRVLDLIA PIGKGQRALI VAPPKTGKTI
MLQRIAQAII QNHPECHVMV VLIDERPEEV TDMRRSIKAE VIASSSDRPT GDHLKVAELA
LERARRLVES GKDVVILLDS ITRLARAYNK EVDSSGRTMT GGVDSRALER PKRIFGAARA
TEEAGSLTII GTALIDTGSR MDEVIFEEFK GTGNSEVTLD RLLAEKRVFP AINIAQSGTR
KEEKLFTLRE YEKVKKLRQM LFSVKPVEAM EALVKRLGRY TYNDEFFDEL
//
