RPOB_SULMW
ID RPOB_SULMW Reviewed; 1328 AA.
AC A8Z5T3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=SMGWSS_057;
OS Sulcia muelleri (strain GWSS).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Candidatus Sulcia.
OX NCBI_TaxID=444179;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GWSS;
RX PubMed=18048332; DOI=10.1073/pnas.0708855104;
RA McCutcheon J.P., Moran N.A.;
RT "Parallel genomic evolution and metabolic interdependence in an ancient
RT symbiosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19392-19397(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_01321}.
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_01321};
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_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000770; ABS30484.1; -; Genomic_DNA.
DR AlphaFoldDB; A8Z5T3; -.
DR SMR; A8Z5T3; -.
DR STRING; 444179.SMGWSS_057; -.
DR PRIDE; A8Z5T3; -.
DR EnsemblBacteria; ABS30484; ABS30484; SMGWSS_057.
DR KEGG; smg:SMGWSS_057; -.
DR HOGENOM; CLU_000524_4_0_10; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000781; 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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 3.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1328
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000329190"
SQ SEQUENCE 1328 AA; 153022 MW; C0979F370B3E5222 CRC64;
MKKIIKIRRF KFPFTKEKTI NFASVRNKIS YPDFLDIQIK SFTNFFCINY TYKNISNKGF
YKVFIEYFPI SDSKNKFIID FISYKIYDPL YSIEECIKRG LTYNVYIRAR FKIYRTRKRK
ITIENKRTKY FETIYQDVYF GTCPYMTPSG SFIFNGSERV IVSQLHRSPG VFFGQYDIPN
LPKISYARII PLKGSWIELS TDINNVMYIY LDIKKRLPIT TLLRALGYTR DIDILNIFNL
AEEVNINKVN YKKFLGRTLA ARIFKTSYQK FEENDILLER NIKLKKYHID IILYYKIKVI
SLYKKNEKNE KNLYYSIIHN TLKKDPTNSQ KEANIYIYKE LKDSFPKNDK KAKLFINKFF
FDETHLGEVG RYKLNKTLKL DFPLKDQILN IEDIISIIEN LIALCNNKKE VDDIDNLANR
RVKTVGEQLY TQYTIGIARV SRIIKERINV KDNETLTPLE LINSKTLTSV INSFFGTDEL
SQFMDQTNPL AEMTHKRRIS SLGPGGLSRE RAGFEIRDVN YSHYGRLCPI ETPEGPNIGL
ISSLCVFAKI NSMGFIETPY FKVKKGKVVI NEAPIYISSD QEYGKLITQA NAILNYKTGV
LKNNIIVRVN ADFPMVNYKK INYIDVSTNQ IASISASLIP FLEHDDANRA LMGSNMMRQS
VPLLNPKAPI VGTGLEKHLA QYVNALIYAE GDGIVESVDA NNIKVKYFNS EKEKLLSFEK
RIKTYKLIKF RKTNQNTCLN IRPIVKKGMY VTKGQVLCEG FATQNGKLAL GRNIKVAFMP
FKGYNFEDAI VISEKVVRED WFTSIHIDEY SLEVRDTKLG MEEFTFDIPN FNEENKKKLD
KYGIIKIGSE VKPGDVLIGR ITPKKEGYPS SEENFLKAIF GKKVGTIKNT SLKADSSLFG
VVIDTKIYSK FSSKEDEQKQ FQIKKLNNKF MKNLKLLRKL LINKLILVLE GSVSEGILNS
SYKEIIPKGK ILNKLNLKKL LKNQEIIYQN WVNNKYKNNL VFKIIKFYYL KINELKIKLK
RKKNRLLIGD EITSGIIKIA KVLIAKKRKL KVGDKMSGRH GNKGIVARIV KEEDMPYLED
GTSVDLVLNP LGVPSRMNLG QIYETILGWA GEKLGINFST PIFDGASIEE ISKYTDIANL
PSFGNTYLFD GETGEKFDQP VTVGVIYMLK LNHMVDDKMH ARSIGPYSLI TQQPLGGKSK
FGGQRLGEME VWALEAFGAA NILREILTVK SDDVKGRTKT YEAIVKRETI PNPGIPESFH
VLLKELKGLG LSLKLEVIKK KEKKNQKIKV RIEIKEKDII KYKKKVKEIK LKKLKELKEQ
LSKSNKKK
