RPOC_PSYA2
ID RPOC_PSYA2 Reviewed; 1406 AA.
AC Q4FQH4;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=Psyc_1886;
OS Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=259536;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17307 / VKM B-2377 / 273-4;
RX PubMed=20154119; DOI=10.1128/aem.02101-09;
RA Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N.,
RA Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C.,
RA Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P.,
RA Murray A., Thomashow M., Tiedje J.M.;
RT "The genome sequence of Psychrobacter arcticus 273-4, a psychroactive
RT Siberian permafrost bacterium, reveals mechanisms for adaptation to low-
RT temperature growth.";
RL Appl. Environ. Microbiol. 76:2304-2312(2010).
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; CP000082; AAZ19734.1; -; Genomic_DNA.
DR RefSeq; WP_011281144.1; NC_007204.1.
DR AlphaFoldDB; Q4FQH4; -.
DR SMR; Q4FQH4; -.
DR STRING; 259536.Psyc_1886; -.
DR EnsemblBacteria; AAZ19734; AAZ19734; Psyc_1886.
DR KEGG; par:Psyc_1886; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000546; 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; -; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1406
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225569"
FT BINDING 72
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 87
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 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 901
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1406 AA; 156049 MW; 531ACFFD2C5D20F6 CRC64;
MKDLLDIMQS PTSNGNHEFD SIQITLASPD VIKSWSHGEV KKPETINYRT FKPERDGLFC
AKIFGPVKDF ECLCGKYKRR KFQGVICEKC GVEVTTAKVR RDRMGHIDLA SPVAHIWFLK
SLPSRIGLLL DMTLRDIERV LYFESYIVTE PGLTSLEKYQ LLDDEDYYKA LEEFGDEFTA
KMGAEAVQDL LKDIDLDLEI DELREAIPQT GSETKLKKMS KRLKLLEAFR NSNNKPEWMV
MNILPVLPPD LRPLVPLEGG RFATSDLNDL YRRVINRNNR LKRLLELSAP DIIVRNEKRM
LQESVDALLD NGRRGRAITG SNKRPLKSLA DMIKGKQGRF RQNLLGKRVD YSGRSVIVVG
PTLRLHQCGL PKKMALELFK PFTYNKLLSH GLATTIKAAK KMVEREEPQV WDMLAMVIRE
HPVLLNRAPT LHRLGLQAFE PVLIEGKAIQ LHPLVCTAFN ADFDGDQMAV HVPLTLEAQL
ESRALMMSTN NILSPANGEP IIVPSQDVVL GLYYISRSSV NAKGEGMIFA TVNEALRAIG
SNDLHVNAKI KVRVTETHID DDGNRTKETS IKDTVAGRLL IWNIMPVGMS FDECNEEMTK
KNISKLINSC YRKVGVKESV MFADQLMYLG FAQATLSGVS IGIDDMVIPP LKKQIIEVAE
AEVREIEDQF EQGFVTAGER YNKVVDIWSR TNDKVAKAMM DNLATDKIIN AKGEEEEQKS
FNSIFIMSDS GARGSAAQIR QLAGMRGLMA KPDGSIIETP IKANFREGLT VLQYFISTHG
ARKGLADTAL KTANSGYLTR RLVDVAQDLV ITSDDCGTEQ GLLMKPHIQG GEIIEKLGEL
VLGRVTARDV TYNDDAEKIL IPAGTLIDEH WVKVLDNNAI DDIWARSVIT CEIEHGVCSQ
CYGRDLARGH KVNIGESVGV MAAQSIGEPG TQLTMRTFHV GGAASSASVD NSISVRSAGQ
AHFENMKTVQ HTDGHLVIVS RSAEIALTDE LGRERERYKV PYGSSVLIKD EEQVEGGQTI
AKWDPHTHPI ITEFAGTARF SEITDGLTAT VKVDDATGMS SFEILATRDR SSSAKDLRPA
IILNTDEGKE VIYFLPAETI IRVSDGEKVA AGSILGRVPQ ASSGTKDITG GLPRVADLFE
ARRPKDHAIM AEMSGVVSFG KETKGKNRFI ITNEDGEIHE ELIPKWRQIN VFENETVARG
EVIADGPQNP HDILRLKGQT ALADYIVNEV QDVYRLQGVK INDKHIEVII RQMLRKVEIT
DGGDSNHFKG DQVEYADIKA LNAKLEAEDK FPVQFERQLL GITKASLATE SFISAASFQE
TTRVLTAAAV TGKVDELRGL KENVVVGRLI PAGTGLAYHK ARKEKAEQKL QDKDLNAAFD
MSATTDSKDF ASFDEAFAQE LNQGNH
