RPOC_ACIBT
ID RPOC_ACIBT Reviewed; 1397 AA.
AC A3M1G4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 83.
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=A1S_0288;
OS Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS KC755 / 5377).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=400667;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX PubMed=17344419; DOI=10.1101/gad.1510307;
RA Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA Gerstein M., Snyder M.;
RT "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT density pyrosequencing and transposon mutagenesis.";
RL Genes Dev. 21:601-614(2007).
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; CP000521; ABO10758.2; -; Genomic_DNA.
DR RefSeq; WP_000653927.1; NZ_CP053098.1.
DR AlphaFoldDB; A3M1G4; -.
DR SMR; A3M1G4; -.
DR GeneID; 66398728; -.
DR KEGG; acb:A1S_0288; -.
DR HOGENOM; CLU_000524_3_1_6; -.
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; -; 1.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..1397
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308816"
FT BINDING 75
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 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 819
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 893
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 900
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 903
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1397 AA; 155051 MW; 197429826058DA14 CRC64;
MKDLLDIMRK KTDSDGHAPV EFDRIRIGLA SPEMIKSWSH GEVKKPETIN YRTFKPERDG
LFCAKIFGPV KDYECLCGKY KRMKYKGVIC EKCGVEVTTA KVRRERMGHI ELASPVAHIW
FLKSLPSRIG LLLDMTLRDI ERVLYFESYV VTDPGMTPFE KYQLLNDEEY FTALEEHGDE
FVAKMGAEAV QDLLKDIDLE AEISRLREEI PQTTSETKLK KASKRLKLME AFKDSNNKPE
WMVMNVLPVL PPDLRPLVPL EGGRFATSDL NDLYRRVINR NNRLKRLLDL AAPDIIVRNE
KRMLQESVDA LLDNGRRGRA ITGSNKRPLK SLADMIKGKQ GRFRQNLLGK RVDYSGRSVI
TVGPTLRLHQ CGLPKKMALE LFKPFIFAKL QASGQATTIK AAKKMVERET PEVWDVLASV
IRQHPVMLNR APTLHRLGLQ AFEPILIEGK AIRLHPLVCA AFNADFDGDQ MAVHVPLTLE
AQLEARALMM STNNILSPAN GEPIIVPSQD VVLGLYYITR DAVNAKGEGM VFADTHEVNR
ALATGQVAIH ARVKVRVHQT VINENGEREQ QTIIVDTTPG RCLLWEVVPE GLSFDMINLE
MTKKNISKLI NSCYRKLGLK DTVIFADQLM YLGFRQATRS GVSVGMEDML IPPTKHTIID
KAETEVREIE QQFEQGFVTA GERYNKVVDI WARTNDQVAK AMMDNLSYTL VKNKQGEDEK
QKSFNSIYMM SDSGARGSAA QIRQLAGMRG LMAKPDGSII ETPIKANFRE GLTVLQYFIS
THGARKGLAD TALKTANSGY LTRRLVDVAQ DLVITEPDCG TSGGLVMTPF IQGGDVIEPL
RDRVLGRVTA EDVRRASDDE VVLPRGTLID EKIAAQLEEA GVDEVKVRSV IACESTFGVC
AKCYGRDLAR GHLVNPGESV GVMAAQSIGE PGTQLTMRTF HVGGAASRTS AANSVQVRNK
GTVRFHNVKT VQHAKGHLVS VSRSGEIGIA DELGRERERY KLPYGASILL KDGELVEAGG
IVATWDPHTH PLVTEVAGKA RFSQIADGVT ATSKTDDATG MTTVEILPVT ARPASGKDLR
PAIVLDTTDG GEQFYFLPQN TIVTVRDGET IGVGDVIGRV PQESSRTRDI TGGLPRVADL
FEARKPKEHA ILAEVSGIVS FGKETKGKNR LVITPDDGSE IYEELIPKWR QINVFEGEHV
NRGETISDGP QNPHDILRLK GEVALTNYIV NEVQDVYRLQ GVKINDKHIE VIVRQMLRKV
DIIDGGDTSF IKGEQVDYIR VVQENQAVLA QNKFPAKFER QLMGITKASL STDSFISAAS
FQETTRVLTE AAVTGKEDDL RGLKENVVVG RLIPAGTGLA YHLERRRQEA EAAEHALHND
FSEVDQAFSQ ALNSEQF
