ID K6VJ17_9MICO Unreviewed; 662 AA.
AC K6VJ17;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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:GAB76729.1};
GN ORFNames=AUCHE_02_00900 {ECO:0000313|EMBL:GAB76729.1};
OS Austwickia chelonae NBRC 105200.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Austwickia.
OX NCBI_TaxID=1184607 {ECO:0000313|EMBL:GAB76729.1, ECO:0000313|Proteomes:UP000008495};
RN [1] {ECO:0000313|EMBL:GAB76729.1, ECO:0000313|Proteomes:UP000008495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105200 {ECO:0000313|EMBL:GAB76729.1,
RC ECO:0000313|Proteomes:UP000008495};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Austwickia chelonae NBRC 105200.";
RL Submitted (AUG-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB76729.1}.
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DR EMBL; BAGZ01000002; GAB76729.1; -; Genomic_DNA.
DR RefSeq; WP_006501480.1; NZ_BAGZ01000002.1.
DR AlphaFoldDB; K6VJ17; -.
DR STRING; 100225.SAMN05421595_1861; -.
DR eggNOG; COG1158; Bacteria.
DR OrthoDB; 9805197at2; -.
DR Proteomes; UP000008495; 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; 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:UP000008495};
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 282..360
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000259|PROSITE:PS51856"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 403..408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 415..420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ SEQUENCE 662 AA; 72446 MW; E5DA63D1134F587C CRC64;
MTDTTELSTP ADEAPKRRGL TTLRLAELQN LAQAMGISGT SGMRKGDLIL AIKERQGGAS
TIDVQVAAPR RTGKVQSTSV SEEKATSDEG TRRSTPSEKT TKDAEPVVKT SAGEVRGTPA
GQDEQPPAGT GRQRRSRRAT APVAAPERRE ETTPAPVEQE KSSSRSEQAE VRQQGAAGNG
ESSQNSDEGQ GRRRSRRERQ RDSRQNGDQS SDSGQSRSDS RGESGQSGGR QSDNRRFGDD
DDSRGGRRRN RQRSRDRKRR GNRGMGDDYS DQMETFTEDD VLVPIAGILD VLDNYAFVRT
SGYLPGPNDV YVPLGIVKKH GLRKGDAVTG AVKALREGEQ LPARQKFNAL VRLDTVNGGA
PDSAKGRVEF NKLTPLYPQE RLRLETEPNI YTTRIIDLVS PIGKGQRGLI VSPPKAGKTL
ILQAIANAIT KNNPEAHLMV VLVDERPEEV TDMQRTVKGE VIASTFDRPA DDHTTVAELA
IERAKRLVEM GHDVVVLLDS ITRLGRAYNL AAPASGRILS GGVDSSALYP PKRFFGAARN
IENGGSLTIL ATALVETGSK MDEVIFEEFK GTGNMELRLS RQLADRRIFP AVDVNPSGTR
REEILMSADE LKLMWKLRRI LSALESQAAL ELLLAQMKKT KQNAEFLMMV QRNSSIKLDD
ED
//
