RPOC2_SYNS9
ID RPOC2_SYNS9 Reviewed; 1364 AA.
AC Q3AZA2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
GN OrderedLocusNames=Syncc9902_0607;
OS Synechococcus sp. (strain CC9902).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=316279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC9902;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Synechococcus sp. CC9902.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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_01324}.
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_01324};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01324};
CC Note=Binds 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01324};
CC -!- SUBUNIT: In cyanobacteria the RNAP catalytic core is composed of 2
CC alpha, 1 beta, 1 beta', 1 gamma and 1 omega subunit. When a sigma
CC factor is associated with the core the holoenzyme is formed, which can
CC initiate transcription. {ECO:0000255|HAMAP-Rule:MF_01324}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. RpoC2
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01324}.
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DR EMBL; CP000097; ABB25575.1; -; Genomic_DNA.
DR RefSeq; WP_011359420.1; NC_007513.1.
DR AlphaFoldDB; Q3AZA2; -.
DR STRING; 316279.Syncc9902_0607; -.
DR EnsemblBacteria; ABB25575; ABB25575; Syncc9902_0607.
DR KEGG; sye:Syncc9902_0607; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_1_0_3; -.
DR OMA; IEGKSDW; -.
DR OrthoDB; 4373at2; -.
DR Proteomes; UP000002712; 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: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; -; 1.
DR HAMAP; MF_01324; RNApol_bact_RpoC2; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
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; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 4.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR TIGRFAMs; TIGR02388; rpoC2_cyan; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase; Zinc.
FT CHAIN 1..1364
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353536"
FT REGION 1318..1342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1320..1334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 324
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 327
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
SQ SEQUENCE 1364 AA; 148333 MW; 6673CAA4264370F4 CRC64;
MTTSKPRKPS KAKAAKAAKA AKAALEKISK PLSKTPPPFR NHIIDKKALK NLVAWSFKHH
GTAVTSSMAD DLKDLGFKYA TQAAVSISVD DLKVPAAKKD LLGQAEEQIT ATEERYRLGE
ITEVERHTKV IDTWTETNER LVDAVKKNFD ENAPLNSVWM MANSGARGNM SQVRQLVGMR
GLMANPQGEI IDLPIRTNFR EGLTVTEYVI SSYGARKGLV DTALRTADSG YLTRRLVDVA
QDVIVREDDC GTMRHIVVEA EDSKFAKRLV GRLTAAQVVS AEGEVLAERD TEIDPALSSK
IEKAGITAVS IRSPLTCEAN RSVCRKCYGW ALAHNELVDL GEAVGIIAAQ SIGEPGTQLT
MRTFHTGGVS TAESGVVRSK VAGDVEFGSK ARVRPYRTPH GVEAQQAEVD FTLTIKPSGK
GRPQKIDITL GSLLFVDNGQ AIESDVTVVQ IAAGAVQKSV EKATKDVICD LAGQVHYEDK
IQPREVTDRQ GNITLKAQRL GRMWVLAGDV YNLPPNALPV VDGKSTVTEG QVLAEASQRS
EFGGDVRLRD SIGDSREVQI VTTAMTLKDF KLLEESNHSG ELWNLEAKDG TRYRLNTIPG
SKIGNGEVIA ELADDRFRTG TGGLVKFAPG LAIKKARSAK NGYEVNKGGT LLWVPQETHE
INKDISLLMI TDGQWIEAGT EVVKDIFSQT AGVVTVTQKN DILREIIVRG GDLRLISDNK
ALERFEGDGQ MVNPGDDVAK GVSVDTMKFV QTVETPEGKG LLLRPVEEYT IPNEAQLPEL
SHLKQANGPH LGIKATQRLA FKDNELIKSV EGVELLKTQL LLETFDTTPQ MTVDVERAPD
KRAKTISRLR LVILESILVR RDTMSDSSHG STHTDLQVED GISVKAGDVV ATTQILCKQE
GVVQLPEATE AEPVRRLIVE RPEDTTTIST SGKPSVAVGD RVVDGDLLAS GQPSDCCGEV
EAVDGSSVTL RLGRPYMVSP DSLLHVRDGD LVQRGDGLAL LVFERQKTGD IVQGLPRIEE
LLEARRPRDS AILCRKPGTV EIKQGEDDDS LSVNVIESDD AIGEYPILLG RNVMVNDGQQ
VTAGELLTDG PINPHELLEC FFEDFRSRKP LMDAAQEAIA NLQHRLVTEV QNVYKSQGVS
IDDKHIEVIV RQMTSKVRVE DAGDTTLLPG ELIELRQVED TNQAMAITGG APSEFTPVLL
GITKASLNTD SFISAASFQE TTRVLTEAAI EGKSDWLRGL KENVIIGRLI PAGTGFSGFE
EELQKEAGPH PDILSEDPAG YRRMQNLRPD YTVDMPPAAS SSALLADPSD ADLEATRTRH
NIDPSASTNA AFTRPDVDNE LKEEQVVDAE AVEGLQEEGL LSDD
