ID W5WIF5_9PSEU Unreviewed; 678 AA.
AC W5WIF5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=KALB_7626 {ECO:0000313|EMBL:AHI00984.1};
OS Kutzneria albida DSM 43870.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kutzneria.
OX NCBI_TaxID=1449976 {ECO:0000313|EMBL:AHI00984.1, ECO:0000313|Proteomes:UP000019225};
RN [1] {ECO:0000313|EMBL:AHI00984.1, ECO:0000313|Proteomes:UP000019225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43870 {ECO:0000313|EMBL:AHI00984.1};
RX PubMed=25301375; DOI=10.1186/1471-2164-15-885;
RA Rebets Y., Tokovenko B., Lushchyk I., Ruckert C., Zaburannyi N.,
RA Bechthold A., Kalinowski J., Luzhetskyy A.;
RT "Complete genome sequence of producer of the glycopeptide antibiotic
RT Aculeximycin Kutzneria albida DSM 43870T, a representative of minor genus
RT of Pseudonocardiaceae.";
RL BMC Genomics 15:885-885(2014).
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; CP007155; AHI00984.1; -; Genomic_DNA.
DR AlphaFoldDB; W5WIF5; -.
DR STRING; 1449976.KALB_7626; -.
DR KEGG; kal:KALB_7626; -.
DR PATRIC; fig|1449976.3.peg.7662; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_3_0_11; -.
DR OrthoDB; 9805197at2; -.
DR Proteomes; UP000019225; 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; 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:UP000019225};
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 300..376
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000259|PROSITE:PS51856"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 419..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 431..436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ SEQUENCE 678 AA; 73799 MW; D54B81CAEDEA5995 CRC64;
MSNTELLGSD AVPAAQGSQQ DSAPAPRTES KETPLTTQSN GTAPRRRAGL SGMVLAELRE
LAGELKIGGT AGMRKGDLIA AIKERQGSSS GRGETAELPL AGVQTASKPA RRTAAEKTAP
KPAVQAEAAP APVVEKAAEP APAAEASAPA AERPATEEEG GRRGNRRRRA ASRPAGSPEG
AEQGEQRQQG DRQQGEPRQN ERQQGEQRQQ GGESRQERGE RGDRGERGNR GDRGDRQRDR
GDRQQGGNRN DRQNDQHDED EDGTGRRGRR FRDRRRNRGS ERPERGQGGG DTEVREDDVL
LPVAGILDVL ENYAFVRTSG YLAGPNDVYV SLSLVRKFGL RRGDNITGVV RQPREGEQQR
QKFNPLVRVD SINGMEPDKV KGRPEFTKLT PLYPNERLRL ETESHILTTR VIDLVMPVGK
GQRALIVSPP KAGKTSVLQA IANAITTNNP ECHLMVVLVD ERPEEVTDMQ RSVHGEVIAS
TFDRPPGDHT SVAELSIERA KRLVEMGHDV VVLLDSITRL GRAYNLAAPA SGRILSGGVD
STALYPPKRF LGAARNIEGG GSLTIFATAL VETGSTMDTV IFEEFKGTGN AELKLDRRIA
DKRVFPAVDV DPSGTRKEEL LLPPDELAVM HKLRRVLHAL DSQQAIDLLL DRLRKSRTNI
EFLMQVAKTT PGSNGNED
//
