ID Q2CJN7_OCEGH Unreviewed; 542 AA.
AC Q2CJN7;
DT 04-APR-2006, integrated into UniProtKB/TrEMBL.
DT 04-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Transcription termination/antitermination protein NusA {ECO:0000256|HAMAP-Rule:MF_00945};
GN Name=nusA {ECO:0000256|HAMAP-Rule:MF_00945};
GN ORFNames=OG2516_11581 {ECO:0000313|EMBL:EAR53102.1};
OS Oceanicola granulosus (strain ATCC BAA-861 / DSM 15982 / KCTC 12143 /
OS HTCC2516).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Oceanicola.
OX NCBI_TaxID=314256 {ECO:0000313|EMBL:EAR53102.1, ECO:0000313|Proteomes:UP000003635};
RN [1] {ECO:0000313|EMBL:EAR53102.1, ECO:0000313|Proteomes:UP000003635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-861 / DSM 15982 / KCTC 12143 / HTCC2516
RC {ECO:0000313|Proteomes:UP000003635};
RX PubMed=20418400; DOI=10.1128/JB.00412-10;
RA Thrash J.C., Cho J.C., Vergin K.L., Giovannoni S.J.;
RT "Genome sequences of Oceanicola granulosus HTCC2516(T) and Oceanicola
RT batsensis HTCC2597(TDelta).";
RL J. Bacteriol. 192:3549-3550(2010).
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}.
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:EAR53102.1}.
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DR EMBL; AAOT01000001; EAR53102.1; -; Genomic_DNA.
DR RefSeq; WP_007255836.1; NZ_CH724107.1.
DR AlphaFoldDB; Q2CJN7; -.
DR STRING; 314256.OG2516_11581; -.
DR eggNOG; COG0195; Bacteria.
DR HOGENOM; CLU_029242_1_2_5; -.
DR OrthoDB; 9807233at2; -.
DR Proteomes; UP000003635; Unassembled WGS sequence.
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; 1.
DR PANTHER; PTHR22648; TRANSCRIPTION TERMINATION FACTOR NUSA; 1.
DR PANTHER; PTHR22648:SF0; TRANSCRIPTION TERMINATION_ANTITERMINATION PROTEIN NUSA; 1.
DR Pfam; PF13184; KH_5; 1.
DR Pfam; PF08529; NusA_N; 1.
DR SMART; SM00322; KH; 1.
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; 1.
DR SUPFAM; SSF69705; Transcription factor NusA, N-terminal domain; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00945};
KW Elongation factor {ECO:0000313|EMBL:EAR53102.1};
KW Protein biosynthesis {ECO:0000313|EMBL:EAR53102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003635};
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 141..207
FT /note="S1 motif"
FT /evidence="ECO:0000259|SMART:SM00316"
FT DOMAIN 308..421
FT /note="K Homology"
FT /evidence="ECO:0000259|SMART:SM00322"
FT REGION 520..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..542
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 542 AA; 60562 MW; 86CED42A1F910A33 CRC64;
MAITSANQLE LLQTAEAVAR EKMIDPGLVV EAMEESLARA AKSRYGAEMD IRVSIDRRTG
RATFTRVRTV VEDEELENYQ AELTVEQAKQ YLDDPKVGDQ YIEEIPPVEL GRIAAQSAKQ
VILQKVREAE RDKQYEEFKD RAGTIINALV KREEYGNVIV DVGAGEAVLR RNEKIGRESY
RPGDRIRCYI KDVRREQRGP QIFLSRTAPE FMAELFKMEV PEIYEGIIEI KAVARDPGSR
AKIGVVSYDG SIDPVGACVG MRGSRVQAVV NELQGEKIDI IPWNEDMPTF LVNALQPAEV
SKVVLDEDAE RIEVVVPEEQ LSLAIGRRGQ NVRLASQLTG LDIDIMTEEE ESKRRQAEFE
ERTKLFMDTL DLDEFFAQLL VSEGFTNLEE VAYVEQDELL VIDGVDEGTA QELQARARDV
LDEQNRVALE KARELGVEDS LVNFEGLTPA MVLALAEDGV KTLEDFATCA DWELAGGWTT
VNGERVKDDG VLEKFDVSLE EAQDMVMTAR VLLGWVDPDD LMPEAAAEDG GEEPSEEEQA
PA
//
