ID   QUEA_STRGC              Reviewed;         342 AA.
AC   A8AYK5;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=S-adenosylmethionine:tRNA ribosyltransferase-isomerase;
DE            EC=2.4.99.17;
DE   AltName: Full=Queuosine biosynthesis protein QueA;
GN   Name=queA; OrderedLocusNames=SGO_1587;
OS   Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 /
OS   DL1 / V288).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=467705;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=17720781; DOI=10.1128/jb.01023-07;
RA   Vickerman M.M., Iobst S., Jesionowski A.M., Gill S.R.;
RT   "Genome-wide transcriptional changes in Streptococcus gordonii in response
RT   to competence signaling peptide.";
RL   J. Bacteriol. 189:7799-7807(2007).
RN   [2]
RP   FUNCTION, INDUCTION, TRANSCRIPTIONAL REGULATION, OPERON STRUCTURE, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=18552185; DOI=10.1128/aem.00556-08;
RA   Liu Y., Dong Y., Chen Y.Y., Burne R.A.;
RT   "Environmental and growth phase regulation of the Streptococcus gordonii
RT   arginine deiminase genes.";
RL   Appl. Environ. Microbiol. 74:5023-5030(2008).
CC   -!- FUNCTION: Transfers and isomerizes the ribose moiety from AdoMet to the
CC       7-aminomethyl group of 7-deazaguanine (preQ1-tRNA) to give
CC       epoxyqueuosine (oQ-tRNA) (By similarity). Seems to have a role in
CC       modulation of ADS (arginine deiminase system) gene expression, perhaps
CC       exerting a negative effect on the translation of arc regulatory
CC       proteins. {ECO:0000250, ECO:0000269|PubMed:18552185}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=7-aminomethyl-7-carbaguanosine(34) in tRNA + S-adenosyl-L-
CC         methionine = adenine + epoxyqueuosine(34) in tRNA + H(+) + L-
CC         methionine; Xref=Rhea:RHEA:32155, Rhea:RHEA-COMP:10342, Rhea:RHEA-
CC         COMP:10346, ChEBI:CHEBI:15378, ChEBI:CHEBI:16708, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:82833, ChEBI:CHEBI:82834;
CC         EC=2.4.99.17;
CC   -!- PATHWAY: tRNA modification; tRNA-queuosine biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- INDUCTION: Is constitutively expressed in the different growth phases.
CC       Its transcription is not subject to carbon catabolite repression (CCR),
CC       and is not affected by arginine or low pH. Is cotranscribed with arcR.
CC       {ECO:0000269|PubMed:18552185}.
CC   -!- DISRUPTION PHENOTYPE: The arcA transcript in QueA-deficient strains is
CC       14-fold more abundant than in the wild-type strain. However, no
CC       significant difference in arginine deiminase (AD) activity (encoded by
CC       arcA) is detected between the wild-type and QueA-deficient strains. The
CC       growth rate of a QueA-deficient strain does not differ significantly
CC       from that of the wild-type strain, but the QueA-deficient strain does
CC       not compete well with the wild-type during serial passage.
CC       {ECO:0000269|PubMed:18552185}.
CC   -!- SIMILARITY: Belongs to the QueA family. {ECO:0000305}.
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DR   EMBL; CP000725; ABV09920.1; -; Genomic_DNA.
DR   RefSeq; WP_012130652.1; NC_009785.1.
DR   AlphaFoldDB; A8AYK5; -.
DR   SMR; A8AYK5; -.
DR   STRING; 467705.SGO_1587; -.
DR   EnsemblBacteria; ABV09920; ABV09920; SGO_1587.
DR   KEGG; sgo:SGO_1587; -.
DR   eggNOG; COG0809; Bacteria.
DR   HOGENOM; CLU_039110_1_0_9; -.
DR   OMA; YSYGDGM; -.
DR   UniPathway; UPA00392; -.
DR   Proteomes; UP000001131; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051075; F:S-adenosylmethionine:tRNA ribosyltransferase-isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 2.40.10.240; -; 1.
DR   Gene3D; 3.40.1780.10; -; 1.
DR   HAMAP; MF_00113; QueA; 1.
DR   InterPro; IPR003699; QueA.
DR   InterPro; IPR042118; QueA_dom1.
DR   InterPro; IPR042119; QueA_dom2.
DR   InterPro; IPR036100; QueA_sf.
DR   PANTHER; PTHR30307; PTHR30307; 1.
DR   Pfam; PF02547; Queuosine_synth; 1.
DR   SUPFAM; SSF111337; SSF111337; 1.
DR   TIGRFAMs; TIGR00113; queA; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Queuosine biosynthesis; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..342
FT                   /note="S-adenosylmethionine:tRNA ribosyltransferase-
FT                   isomerase"
FT                   /id="PRO_0000418335"
SQ   SEQUENCE   342 AA;  38138 MW;  278191D8760B18EC CRC64;
     MNTADFDFHL PEELIAQTPL EKRDASRLLV VDRSSGEFSD QHFDSIIDQL QPGDALVMNN
     TRVLPARLYG EKPGTGGHVE LLLLKNTEGD QWEVLAKPAK RLKVGAQVSF GDGRLTATVV
     DELEHGGRIV RFDYQGIFLE VLESLGEMPL PPYIHEKLAD RERYQTVYAK ENGSAAAPTA
     GLHFTKELLA QIEAKGVKLV YLTLHVGLGT FRPVSVDNLD DHEMHSEFYT LSEEAAATLR
     EVKANGHRVI AVGTTSIRTL ETIGNKFKGD IQADSGWTNI FIKPGYQWQI VDAFSTNFHL
     PKSTLVMLVS AFAGRDLTLK AYEHAIAERY RFFSFGDAMF IK