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Database: UniProt
Entry: K0B0H1_CLOA9
LinkDB: K0B0H1_CLOA9
Original site: K0B0H1_CLOA9 
ID   K0B0H1_CLOA9            Unreviewed;       359 AA.
AC   K0B0H1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   10-APR-2019, entry version 46.
DE   RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000256|HAMAP-Rule:MF_00945};
GN   Name=nusA {ECO:0000256|HAMAP-Rule:MF_00945,
GN   ECO:0000313|EMBL:AFS78567.1};
GN   OrderedLocusNames=Curi_c15580 {ECO:0000313|EMBL:AFS78567.1};
OS   Clostridium acidurici (strain ATCC 7906 / DSM 604 / BCRC 14475 / CIP
OS   104303 / NCIMB 10678 / 9a) (Gottschalkia acidurici).
OC   Bacteria; Firmicutes; Tissierellia; Tissierellales; Gottschalkiaceae;
OC   Gottschalkia.
OX   NCBI_TaxID=1128398 {ECO:0000313|EMBL:AFS78567.1, ECO:0000313|Proteomes:UP000006094};
RN   [1] {ECO:0000313|EMBL:AFS78567.1, ECO:0000313|Proteomes:UP000006094}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7906 / DSM 604 / BCRC 14475 / CIP 104303 / NCIMB 10678 /
RC   9a {ECO:0000313|Proteomes:UP000006094};
RX   PubMed=23240052; DOI=10.1371/journal.pone.0051662;
RA   Hartwich K., Poehlein A., Daniel R.;
RT   "The purine-utilizing bacterium Clostridium acidurici 9a: a genome-
RT   guided metabolic reconsideration.";
RL   PLoS ONE 7:E51662-E51662(2012).
CC   -!- FUNCTION: Participates in both transcription termination and
CC       antitermination. {ECO:0000256|HAMAP-Rule:MF_00945}.
CC   -!- SUBUNIT: Monomer. Binds directly to the core enzyme of the DNA-
CC       dependent RNA polymerase and to nascent RNA. {ECO:0000256|HAMAP-
CC       Rule:MF_00945}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945}.
CC   -!- SIMILARITY: Belongs to the NusA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00945}.
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DR   EMBL; CP003326; AFS78567.1; -; Genomic_DNA.
DR   RefSeq; WP_014967703.1; NC_018664.1.
DR   STRING; 1128398.Curi_c15580; -.
DR   EnsemblBacteria; AFS78567; AFS78567; Curi_c15580.
DR   KEGG; cad:Curi_c15580; -.
DR   PATRIC; fig|1128398.3.peg.1594; -.
DR   KO; K02600; -.
DR   OMA; SRTTPKM; -.
DR   OrthoDB; 384865at2; -.
DR   Proteomes; UP000006094; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-UniRule.
DR   GO; GO:0031564; P:transcription antitermination; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1480.10; -; 1.
DR   Gene3D; 3.30.300.20; -; 2.
DR   HAMAP; MF_00945_B; NusA_B; 1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR015946; KH_dom-like_a/b.
DR   InterPro; IPR025249; KH_dom_NusA-like.
DR   InterPro; IPR009019; KH_sf_prok-type.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR030842; NusA_bac.
DR   InterPro; IPR036555; NusA_N_sf.
DR   InterPro; IPR022967; S1_dom.
DR   InterPro; IPR003029; S1_domain.
DR   InterPro; IPR013735; TF_NusA_N.
DR   InterPro; IPR010213; Tscrpt_termination_fac_NusA.
DR   PANTHER; PTHR22648; PTHR22648; 1.
DR   Pfam; PF13184; KH_5; 1.
DR   Pfam; PF08529; NusA_N; 1.
DR   Pfam; PF00575; S1; 1.
DR   SMART; SM00322; KH; 2.
DR   SMART; SM00316; S1; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF54814; SSF54814; 2.
DR   SUPFAM; SSF69705; SSF69705; 1.
DR   TIGRFAMs; TIGR01953; NusA; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006094};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Elongation factor {ECO:0000313|EMBL:AFS78567.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:AFS78567.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006094};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription antitermination {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription regulation {ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription termination {ECO:0000256|HAMAP-Rule:MF_00945}.
FT   DOMAIN      135    199       S1 motif. {ECO:0000259|PROSITE:PS50126}.
FT   COILED      104    124       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   359 AA;  40426 MW;  989DAA68DDDFC5E0 CRC64;
     MKAEFIEALE EIEKEKGISK ELIFEALEAA LISGYKKNFG SSQNVEVDVN KETGDVKLYA
     KKNVVEIVED ELLDISIEEA KKLDANYELE DIVRVEITPR NFGRIAAQTA KQVVMQKIKE
     AEREIVFDEF INRENEIITG IVQRASKNNI LIDLGKTEGI LAPSEQIQGE EYNQGDRIKS
     YILEVKKTTK GPQILLSRTH PGLVKRLFEL EVPEIQEGIV DIYNISREAG SRTKIAVYSN
     DENVDPVGAC VGFKGARVKA IVDELYGEKI DIITWDKDIK EFIQNSLSPA KVVKVEVDEK
     EKSALVVVPD YQLSLAIGKE GQNARLAAKL TNWKIDIKSE SQYNSEIHSD EELIDNIEN
//
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