RPOC_FUSNN
ID RPOC_FUSNN Reviewed; 1319 AA.
AC Q8RHI7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=FN2035;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; AE009951; AAL94120.1; -; Genomic_DNA.
DR RefSeq; NP_602821.1; NC_003454.1.
DR AlphaFoldDB; Q8RHI7; -.
DR SMR; Q8RHI7; -.
DR STRING; 190304.FN2035; -.
DR PRIDE; Q8RHI7; -.
DR EnsemblBacteria; AAL94120; AAL94120; FN2035.
DR KEGG; fnu:FN2035; -.
DR PATRIC; fig|190304.8.peg.498; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR InParanoid; Q8RHI7; -.
DR OMA; YRNIRVE; -.
DR BioCyc; FNUC190304:G1FZS-522-MON; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 2.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 1.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1319
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067745"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 773
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 846
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 853
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 856
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1319 AA; 148103 MW; 7F57DE94BA472B85 CRC64;
MGIRNFEKIR IKLASPEKIL EWSHGEVTKP ETINYRTLNP ERDGLFCEII FGPTKDWECS
CGKYKRMRYK GLVCEKCGVE VTRAKVRRER MGHITLASPV SHIWYSKGSP NKMSLIIGIS
SKELESVLYF ARYIVTSSQE STVEVGKILT EKEYKLLKQL YGNKFEAYMG ADGILKLLTA
IDLEKLRDEL ENELAEANSA QKRKKLVKRL KIVRDFIASG NRPEWMILTN VPVIPAELRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLKK LLEIRAPEIV VKNEKRMLQE AVDALIDNGR
RGKPVVAQNN RELKSLSDML KGKQGRFRQN LLGKRVDYSA RSVIVVGPSL KMNQCGIPKK
MALELYKPFI MRELVRRELA NNIKMAKKLV EESDDKVWAV IEDVIADHPV LLNRAPTLHR
LSIQAFQPVL IEGKAIRLHP LVCSAFNADF DGDQMAVHLT LSPESMMEAK LLMFAPNNII
SPSSGEPIAV PSQDMVMGCF YMTKERPGEK GEGKLFSNIE QVITAYQNDK VGTHALIKVR
MNGELIETTP GRVLFNEILP EIDRNYHKTY GKKEIKSLIK SLYEAHGFTE TAELINRVKN
FGYHYGTFAG VSVGIEDLEV PPKKKSLLNQ ADKEVAQIDK DYKSGKIINE ERYRKTIEVW
SRTTEAVTDA MMKNLDEFNP VYMMATSGAR GNVSQMRQLA GMRGNMADTQ GRTIEVPIKA
NFREGLTVLE FFMSSHGARK GLADTALRTA DSGYLTRRLV DISHEVIVNE EDCHTHEGIE
VEALVGANGK IIEKLSERIN GRVLAEDLVH KGKKIAKRNT MIHKDLLDKI EELGIKKVKI
RSPLTCALEK GVCQKCYGMD LSNYNEILLG EAVGVVAAQS IGEPGTQLTM RTFHTGGVAG
AATVVNSKKA ENDGEVSFRD IKTIEINGED VVVSQGGKII IADNEHEVDS GSVIRVTEGQ
KVKEGDVLVT FDPYHIPIIS SHDGKVQYRH FTPKNIRDEK YDVHEYLVVR SVDSVDSEPR
VHILDKKNEK LATYNIPYGA YMMVRDGAKV KKGDIIAKII KLGEGTKDIT GGLPRVQELF
EARNPKGKAT LAEIDGRIEI LTTKKKQMRV VNVRSLENPE EFKEYLIPMG ERLVVTDGLK
IKAGDKITEG AISPYDVLNI KGLVAAEQFI LESVQQVYRD QGVTVNDKHI EIIVKQMFRK
VRIIDSGASL FLEDEVIEKR VVDLENKKLE EQGKALIKYE PVIQGITKAA VNTGSFISAA
SFQETTKVLS NAAIEGKVDY LEGLKENVIL GKKIPAGTGF NKYKSIKVRY NTDDKPEEE
