ID   SYV_CHLPN               Reviewed;         940 AA.
AC   Q9Z987; Q9JQA5;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02004};
DE   AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02004};
DE            Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   Name=valS {ECO:0000255|HAMAP-Rule:MF_02004};
GN   OrderedLocusNames=CPn_0094, CP_0680, CpB0094;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT   Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can
CC       inadvertently accommodate and process structurally similar amino acids
CC       such as threonine, to avoid such errors, it has a 'posttransfer'
CC       editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-
CC       dependent manner. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-
CC         tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-
CC         COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02004};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: ValRS has two distinct active sites: one for aminoacylation and
CC       one for editing. The misactivated threonine is translocated from the
CC       active site to the editing site. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain is crucial for aminoacylation
CC       activity. {ECO:0000255|HAMAP-Rule:MF_02004}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       ValS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_02004}.
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DR   EMBL; AE001363; AAD18247.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF38490.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA98304.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98027.1; -; Genomic_DNA.
DR   PIR; B72120; B72120.
DR   PIR; F86502; F86502.
DR   RefSeq; NP_224302.1; NC_000922.1.
DR   RefSeq; WP_010882744.1; NZ_LN847257.1.
DR   AlphaFoldDB; Q9Z987; -.
DR   SMR; Q9Z987; -.
DR   STRING; 115711.CP_0680; -.
DR   PRIDE; Q9Z987; -.
DR   EnsemblBacteria; AAD18247; AAD18247; CPn_0094.
DR   EnsemblBacteria; AAF38490; AAF38490; CP_0680.
DR   GeneID; 45050139; -.
DR   KEGG; cpa:CP_0680; -.
DR   KEGG; cpj:valS; -.
DR   KEGG; cpn:CPn_0094; -.
DR   KEGG; cpt:CpB0094; -.
DR   PATRIC; fig|115713.3.peg.107; -.
DR   eggNOG; COG0525; Bacteria.
DR   HOGENOM; CLU_001493_0_2_0; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004832; F:valine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd07962; Anticodon_Ia_Val; 1.
DR   Gene3D; 1.10.287.380; -; 1.
DR   Gene3D; 3.40.50.620; -; 2.
DR   HAMAP; MF_02004; Val_tRNA_synth_type1; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR002300; aa-tRNA-synth_Ia.
DR   InterPro; IPR033705; Anticodon_Ia_Val.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR010978; tRNA-bd_arm.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR037118; Val-tRNA_synth_C_sf.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   InterPro; IPR002303; Valyl-tRNA_ligase.
DR   PANTHER; PTHR11946; PTHR11946; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   PRINTS; PR00986; TRNASYNTHVAL.
DR   SUPFAM; SSF46589; SSF46589; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00422; valS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Coiled coil; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..940
FT                   /note="Valine--tRNA ligase"
FT                   /id="PRO_0000106221"
FT   COILED          873..905
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
FT   MOTIF           47..57
FT                   /note="'HIGH' region"
FT   MOTIF           564..568
FT                   /note="'KMSKS' region"
FT   BINDING         567
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02004"
SQ   SEQUENCE   940 AA;  107111 MW;  28054683FB9D0404 CRC64;
     MTTEDFPKAY NFQDTEPELY VFWEKNGMFK AEASSDKPPY SVIMPPPNVT GVLHMGHALV
     NTLQDVLVRY KRMSGFEVCW IPGTDHAGIA TQAVVERHLQ ASEGKRRTDY SREDFLKHIW
     AWKEKSEKVV LSQLRQLGCS CDWDRKRFTM EPLANRAVKK AFKTLFENGY IYRGYYLVNW
     DPVLQTALAD DEVEYEEKDG WLYYIRYRMV GSQESIVVAT TRPETSLGDT GIAVSPNDER
     YASWIGASVE VPFVNRQIPI IGDASVDPTF GTGAVKVTPA HDKDDYLMGT NHHLPMINIL
     TPSGGINENG GPFAGMAKEK AREEILIALE EQGLFVRKEP YKLRVGVSYR SGAVIEPYLS
     KQWFVSVSEF RGALREFVES QDIKIFPKDF VKNYLSWVNH LRDWCISRQL WWGHRIPVWY
     HKNDDERVLC YDGEGIPEEV AQDPDSWYQD PDVLDTWFSS GLWPLTCLGW PDENSPDLKK
     FYPTALLVTG HDILFFWVTR MVLLCSSMSG EKPFSEVFLH GLIFGKSYKR YNDFGEWSYI
     SGKEKLAYDM GEALPDGVVA KWEKLSKSKG NVIDPLEMIA TYGTDAVRLT LCSCANRGEQ
     IDLDYRLFEE YKHFANKVWN GARFIFGHIS DLQGKDLLAG IDEDSLGLED FYILDGFNQL
     IHQLEEAYAT YAFDKVATLA YEFFRNDLCS TYIEIIKPTL FGKQGNEASQ STKRTLLAVL
     LINVLGVLHP VAPFITESLF LRIQDTLGAL PEGDGDAFTG HALRMLRSRA CMEAPYPKAF
     DVKIPQDLRE SFTLAQRLVY TIRNIRGEMQ LDPRLHLKAF VVCSDTTEIQ SCIPILQALG
     GLESIQLLDK EPEKGLYSFG VVDTIRLGIF VPEEHLLKEK GRLEKERVRL ERAVENLERL
     LGDESFCQKA NPNLVVAKQE ALKNNRIELQ GILDKLASFA