ID   RF1_BARQU               Reviewed;         359 AA.
AC   Q6G0R0;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=BQ01850;
OS   Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283165;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Toulouse;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF25688.1; -; Genomic_DNA.
DR   RefSeq; WP_011179003.1; NC_005955.1.
DR   AlphaFoldDB; Q6G0R0; -.
DR   SMR; Q6G0R0; -.
DR   STRING; 283165.BQ01850; -.
DR   EnsemblBacteria; CAF25688; CAF25688; BQ01850.
DR   KEGG; bqu:BQ01850; -.
DR   eggNOG; COG0216; Bacteria.
DR   HOGENOM; CLU_036856_0_1_5; -.
DR   OMA; ISDHRVG; -.
DR   OrthoDB; 928964at2; -.
DR   Proteomes; UP000000597; 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_0000177636"
FT   REGION          284..311
FT                   /note="Disordered"
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;  40356 MW;  DFED35C7F0A5C966 CRC64;
     MVSLPKDRMR QLEKRFEIIE SQMAKNPDSG TYVKLASEYA DLQPIVTSIR TLNALSIEIT
     ELETIISDKL TDVEMRNLAQ EELPPLFQKM EKLEKELQIL LLPKDITDEK SAIIEIRAGT
     GGSEAALFVG DLFRMYERYA NAYNWKVEVI SLNEGEVGGY KEIIATISGK GVFSKLKFES
     GVHRVQRVPE TETSGRIHTS AATVAVLPEA EEIDIEIRPE DIRIDTMRAS GAGGQHVNTT
     DSAVRITHIP TGIMVVQAEK SQHQNRARAL QILRARLFDI EQKKAESERS ASRKNQVGSG
     DRSERIRTYN FPQGRVTDHR INLTLYKLDR ILEGDLDELI NALISDYQTA LLTEMDGNG