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Database: UniProt
Entry: K0C2P2_CYCSP
LinkDB: K0C2P2_CYCSP
Original site: K0C2P2_CYCSP 
ID   K0C2P2_CYCSP            Unreviewed;       500 AA.
AC   K0C2P2;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
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:AFT67614.1};
GN   OrderedLocusNames=Q91_1579 {ECO:0000313|EMBL:AFT67614.1};
OS   Cycloclasticus sp. (strain P1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Cycloclasticus.
OX   NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT67614.1, ECO:0000313|Proteomes:UP000006282};
RN   [1] {ECO:0000313|EMBL:AFT67614.1, ECO:0000313|Proteomes:UP000006282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1 {ECO:0000313|EMBL:AFT67614.1,
RC   ECO:0000313|Proteomes:UP000006282};
RX   PubMed=23144416; DOI=10.1128/JB.01837-12;
RA   Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT   "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus
RT   sp. strain P1.";
RL   J. Bacteriol. 194:6677-6677(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; CP003230; AFT67614.1; -; Genomic_DNA.
DR   RefSeq; WP_015006384.1; NC_018697.1.
DR   AlphaFoldDB; K0C2P2; -.
DR   STRING; 385025.Q91_1579; -.
DR   KEGG; cyq:Q91_1579; -.
DR   PATRIC; fig|385025.3.peg.1615; -.
DR   HOGENOM; CLU_029242_0_0_6; -.
DR   Proteomes; UP000006282; 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:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
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   CDD; cd02134; KH-II_NusA_rpt1; 1.
DR   CDD; cd22529; KH-II_NusA_rpt2; 1.
DR   CDD; cd04455; S1_NusA; 1.
DR   Gene3D; 3.30.300.20; -; 2.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.30.1480.10; NusA, N-terminal domain; 1.
DR   HAMAP; MF_00945_B; NusA_B; 1.
DR   InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
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; IPR003029; S1_domain.
DR   InterPro; IPR013735; TF_NusA_N.
DR   InterPro; IPR010214; Tscrpt_termin_fac_NusA_C_rpt.
DR   InterPro; IPR010213; Tscrpt_termination_fac_NusA.
DR   NCBIfam; TIGR01953; NusA; 1.
DR   NCBIfam; TIGR01954; nusA_Cterm_rpt; 2.
DR   PANTHER; PTHR22648; TRANSCRIPTION TERMINATION FACTOR NUSA; 1.
DR   PANTHER; PTHR22648:SF0; TRANSCRIPTION TERMINATION_ANTITERMINATION PROTEIN NUSA; 1.
DR   Pfam; PF14520; HHH_5; 2.
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; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF54814; Prokaryotic type KH domain (KH-domain type II); 2.
DR   SUPFAM; SSF47794; Rad51 N-terminal domain-like; 2.
DR   SUPFAM; SSF69705; Transcription factor NusA, N-terminal domain; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50126; S1; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00945};
KW   Elongation factor {ECO:0000313|EMBL:AFT67614.1};
KW   Protein biosynthesis {ECO:0000313|EMBL:AFT67614.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006282};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00945};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00945};
KW   Transcription antitermination {ECO:0000256|ARBA:ARBA00022814,
KW   ECO:0000256|HAMAP-Rule:MF_00945};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_00945};
KW   Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW   ECO:0000256|HAMAP-Rule:MF_00945}.
FT   DOMAIN          143..208
FT                   /note="S1 motif"
FT                   /evidence="ECO:0000259|PROSITE:PS50126"
SQ   SEQUENCE   500 AA;  55740 MW;  C7A266A6FD628FDE CRC64;
     MANKEILMVV DVVSNEKEID RSVLFEAIEA ALEMATKKLY RDDIAVRVAI DRVSGDYESF
     RQWEVVEADP EFENGLENPD AQILLEDAQK KDPTLEVGSF IEEPIESADF GRIGAQAAKQ
     VIVQKVREAE RRKVYELYKD KVGELVTGVI KRIERGNVFV DLEGTADAII PREEMIPREP
     VRTGDRIRGY LKSVEEVTRG PQLTVSRSAP ELLTALFKLE VPEVGDGLIE ILGAARDPGS
     RAKIAVRTRD QRLDPVGACV GMRGSRVQAV SNELAGERVD IILWDENEAQ FVINAMSPAE
     VVAIVVDEDK HSMDVSVKDD SLSQAIGRGG QNVRLASELT GWKLNVMSET QADEQNSSEA
     DGYAQQLMLD LDVDEDVALI LVQEGYTSIE EINFADLDDL TDIEEFDEDI AEELQQRAKD
     AYLIKAIASE EVLEEHEPAK DLLNMEGMDR ELAFKLASKE IVTMEDLANL ATDELLEIAS
     IDEERATTLI MKAREPWFAE
//
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