ID   RF1_CHLTA               Reviewed;         359 AA.
AC   Q3KMZ9;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Peptide chain release factor 1 {ECO:0000255|HAMAP-Rule:MF_00093};
DE            Short=RF-1 {ECO:0000255|HAMAP-Rule:MF_00093};
GN   Name=prfA {ECO:0000255|HAMAP-Rule:MF_00093}; OrderedLocusNames=CTA_0025;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
CC   -!- FUNCTION: Peptide chain release factor 1 directs the termination of
CC       translation in response to the peptide chain termination codons UAG and
CC       UAA. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- PTM: Methylated by PrmC. Methylation increases the termination
CC       efficiency of RF1. {ECO:0000255|HAMAP-Rule:MF_00093}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000255|HAMAP-Rule:MF_00093}.
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DR   EMBL; CP000051; AAX50273.1; -; Genomic_DNA.
DR   RefSeq; WP_009871370.1; NC_007429.1.
DR   AlphaFoldDB; Q3KMZ9; -.
DR   SMR; Q3KMZ9; -.
DR   EnsemblBacteria; AAX50273; AAX50273; CTA_0025.
DR   KEGG; cta:CTA_0025; -.
DR   HOGENOM; CLU_036856_0_1_0; -.
DR   OMA; ISDHRVG; -.
DR   Proteomes; UP000002532; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00093; Rel_fac_1; 1.
DR   InterPro; IPR005139; PCRF.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   InterPro; IPR004373; RF-1.
DR   Pfam; PF03462; PCRF; 1.
DR   Pfam; PF00472; RF-1; 1.
DR   SMART; SM00937; PCRF; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   TIGRFAMs; TIGR00019; prfA; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methylation; Protein biosynthesis.
FT   CHAIN           1..359
FT                   /note="Peptide chain release factor 1"
FT                   /id="PRO_0000263250"
FT   REGION          287..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         235
FT                   /note="N5-methylglutamine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00093"
SQ   SEQUENCE   359 AA;  40052 MW;  0ED087BCC230CE7A CRC64;
     MEIKVLECLK RLEEVEKQIS DPNIFSNPKE YSSLSKEHAR LSEIKNAHES LVATKKILQD
     DKLALSTEKD PEIVAMLEEG VLVGEEAVER LSKQLENLLI PPDPDDDLSV IMELRAGTGG
     DEAALFVGDC VRMYHLYAAS KGWQCEVLST SESDLGGYKE YVMGISGASV KRFLQYEAGT
     HRVQRVPETE TQGRVHTSAV TVAVLPEPAE DDEEVFIDEK DLRIDTFRSS GAGGQHVNVT
     DSAVRITHIP SGVVVTCQDE RSQHKNKAKA MRVLKARIRD AEVQKRAQEA SAMRSAQVGS
     GDRSERIRTY NFPQNRVTDH RIGLTLYNLD RVMEGELDMI TTALVTHVHR QLFGHEETA