RPOC2_PHAVU
ID RPOC2_PHAVU Reviewed; 1366 AA.
AC A4GGA7; A8W810;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=DNA-directed RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=PEP {ECO:0000255|HAMAP-Rule:MF_01324};
DE AltName: Full=Plastid-encoded RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
DE Short=RNA polymerase subunit beta'' {ECO:0000255|HAMAP-Rule:MF_01324};
GN Name=rpoC2 {ECO:0000255|HAMAP-Rule:MF_01324};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Negro Jamapa;
RX PubMed=17623083; DOI=10.1186/1471-2164-8-228;
RA Guo X., Castillo-Ramirez S., Gonzalez V., Bustos P.,
RA Fernandez-Vazquez J.L., Santamaria R.I., Arellano J., Cevallos M.A.,
RA Davila G.;
RT "Rapid evolutionary change of common bean (Phaseolus vulgaris L) plastome,
RT and the genomic diversification of legume chloroplasts.";
RL BMC Genomics 8:228-228(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Moore M.J., Triplett E.W., Broughton W.J., Soltis P.S., Soltis D.E.;
RT "Complete nucleotide sequence of the plastid genome of the common bean,
RT Phaseolus vulgaris.";
RL Submitted (OCT-2007) 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 plastids the minimal PEP RNA polymerase catalytic core is
CC composed of four subunits: alpha, beta, beta', and beta''. When a
CC (nuclear-encoded) sigma factor is associated with the core the
CC holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01324}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255|HAMAP-
CC 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; DQ886273; ABH88088.1; -; Genomic_DNA.
DR EMBL; EU196765; ABW22780.1; -; Genomic_DNA.
DR RefSeq; YP_001122808.1; NC_009259.1.
DR AlphaFoldDB; A4GGA7; -.
DR GeneID; 4961803; -.
DR KEGG; pvu:PhvuCp24; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; 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; 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 Chloroplast; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Plastid; Transcription; Transferase; Zinc.
FT CHAIN 1..1366
FT /note="DNA-directed RNA polymerase subunit beta''"
FT /id="PRO_0000353580"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 298
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01324"
FT CONFLICT 751..755
FT /note="NSKGS -> IQKDQ (in Ref. 2; ABW22780)"
FT /evidence="ECO:0000305"
FT CONFLICT 993
FT /note="L -> W (in Ref. 2; ABW22780)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1366 AA; 156371 MW; 013EAD185DBA5357 CRC64;
MAERTNLMFH NKVIGGTAIK RLISRLIDHF GMAYTSHILD QVKTLGFRQA TATSISLGID
DLLTIPSKGW LVRDAEHQNL ILEKQHHYGN VHAVEKLRQS IEIWYATSEY FRQEMNPNFR
MTDPFNPVHI MSFSGARGNA SQVHQLVGMR GLMSDPQGQM IDLPIQSNLR EGLSLTEYII
SCYGARKGVV DTAVRTSDAG YLTRRLVEVV QHIVIRRTDC GTIRGISVNT QNEMMPESTW
TQTLIGRVLA DDIYRGSRCI AVRNQDIGIG LFNQFKTFQT QPISIRTPFT CRNTSWICRL
CYGQSPTQGH LVELGEAVGI IAGQSIGEPG TQLTLRTFHT GGVFTGGTAE QVRAPYNGKI
KFNEDLVHPT RTRHGHPAFL CYIDLYVSIE NGDIIHNVTI PPKSFLLVQN NQYVKSEQVI
AEILAGTYTF NFKEKVRKHV YSDLEGEMHW STNVYHASEF KYSNVHILPK TSHLWILSGK
SDRSGSVSFS TRKDQDQLNI HSLSTGERDI CNHLASNNKI RHKLFHFNPS EKKERRISDY
SIINQIICID HCHFTHPAIF HDTTDLLAKR RRNRFIIPFQ FQSIQERDKA LMLASSISIE
IPINGLFRRN SIFAYFDDPQ YRTQSSGITK YRTIDINYIL KKEDFVIEYP GVKEFKTKYQ
MKVDQFFFIP EEVYILPEFS SIMVRNNSIV EVDTPITVNI RSQVSGLVRL EKKKKKIQLK
IFSGNIYFPG EMDKISRHSA MLIPPRTVKK NSKGSKKKMK NWIYAQWITI TKKKYFVLVR
PVILYEIADR IKLIKFFSQD MLQERDNLEL QVINYILSGN GKSIRGISNT SIQLVRTCLV
LNWDQDKKVS SIEKGHASFV ELSINGLVRY FLKIALVKSH ISYIRKRNDP SGSRFILDNE
SDWTNINPFF SMNSREKVQQ SLSQNHGTIH MLLNRNDKCR SLIILSSSNC FQIRSFHDGK
YYKEEMNPIQ RDPLIPIKNS LGPLGIALQV ANLDFYLLIT HNQISINKNG QLDKLKETFQ
VFKYYLIDEN ERIYKPDISS NILLNPFYLN WHFFHHNSCE KKTFPIISLG QFICENVCIV
QMKNAPHLKS GQILTVQMDS VGIRSANPYL ATPGTTVHGH YGEILSEGDI LVTFIYQKSR
SGDITQGLPK VEQVLEVRSI DSISINLEKR VGTWNGRITR ILGIPWGFFI SAELTIAQSR
ISLVNQIQKV YRSQGVHIHN RHIEIIVRQI TSKVLVSEDG MSNVFLPGEL IGLLRAERAG
RSLEESICYR VLLLGITKTS LNTQSFISEA SFQETARVLS KAALRGRIDW LKGLKENVVL
GGMMPVGTGF KRIIYRSKQR QYNKITSETK KRIDMIYQSN LGFKNS
