ID A0A2U1SX04_9MICO Unreviewed; 369 AA.
AC A0A2U1SX04;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Peptide chain release factor 2 {ECO:0000256|HAMAP-Rule:MF_00094};
DE Short=RF-2 {ECO:0000256|HAMAP-Rule:MF_00094};
GN Name=prfB {ECO:0000256|HAMAP-Rule:MF_00094};
GN ORFNames=DF220_12370 {ECO:0000313|EMBL:PWB96165.1};
OS Salinibacterium hongtaonis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Salinibacterium.
OX NCBI_TaxID=2079791 {ECO:0000313|EMBL:PWB96165.1, ECO:0000313|Proteomes:UP000244978};
RN [1] {ECO:0000313|Proteomes:UP000244978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S1194 {ECO:0000313|Proteomes:UP000244978};
RA Liu S., Wang Z., Li J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Peptide chain release factor 2 directs the termination of
CC translation in response to the peptide chain termination codons UGA and
CC UAA. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- PTM: Methylated by PrmC. Methylation increases the termination
CC efficiency of RF2. {ECO:0000256|HAMAP-Rule:MF_00094}.
CC -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC family. {ECO:0000256|ARBA:ARBA00010835, ECO:0000256|HAMAP-
CC Rule:MF_00094}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWB96165.1}.
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DR EMBL; QEEX01000002; PWB96165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1SX04; -.
DR KEGG; salc:C2138_03660; -.
DR Proteomes; UP000244978; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.70.1660; -; 1.
DR Gene3D; 1.20.58.410; Release factor; 1.
DR HAMAP; MF_00094; Rel_fac_2; 1.
DR InterPro; IPR005139; PCRF.
DR InterPro; IPR000352; Pep_chain_release_fac_I.
DR InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR InterPro; IPR004374; PrfB.
DR NCBIfam; TIGR00020; prfB; 1.
DR PANTHER; PTHR43116; PEPTIDE CHAIN RELEASE FACTOR 2; 1.
DR PANTHER; PTHR43116:SF3; RF_PROK_I DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03462; PCRF; 1.
DR Pfam; PF00472; RF-1; 1.
DR SMART; SM00937; PCRF; 1.
DR SUPFAM; SSF75620; Release factor; 1.
DR PROSITE; PS00745; RF_PROK_I; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00094};
KW Methylation {ECO:0000256|ARBA:ARBA00022481, ECO:0000256|HAMAP-
KW Rule:MF_00094}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00094};
KW Reference proteome {ECO:0000313|Proteomes:UP000244978}.
FT DOMAIN 244..260
FT /note="Prokaryotic-type class I peptide chain release
FT factors"
FT /evidence="ECO:0000259|PROSITE:PS00745"
FT COILED 69..115
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 251
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00094"
SQ SEQUENCE 369 AA; 40386 MW; AD1A2FB06641D574 CRC64;
MDELDISAQV ATLRATFTEI TAVVDVDRLT ADIATLSEQA GVPDLWDDPA AAQKVTSALS
HRQAELAKIK GLKQRLDDIE IMVELANEEG DADAAAEVHK ELRDIQRVLG ELEVQTLLNG
EWDSRAAVMT IRSGAGGVDA ADFAEMLQRM YLRYAEKAGI PARVLDTSYA EEAGIKSTTI
EFDAPYAFGK LSVEAGTHRL VRMSPFGAAG KRQTSFAAVE VIPLMEETES IEIPENEIRV
DVFRSSGPGG QSVNTTDSAV RLTHIPTGIV VSMQNEKSQI QNRAAAMRVL QSRLLLVQKE
QEAAQKKELA GTITASWGDQ MRSYVLAPYQ MVKDLRTEYE VGNPSNVFDG DLDGFITAGI
RWRKRAVES
//
