ID   SYP_ACIC5               Reviewed;         585 AA.
AC   C1F3P3;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   04-NOV-2026, entry version 87.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569};
DE            Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569};
GN   Name=proS {ECO:0000255|HAMAP-Rule:MF_01569};
GN   OrderedLocusNames=ACP_2832;
OS   Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS   7670 / NBRC 15755 / NCIMB 13165 / 161).
OC   Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia; Terriglobales;
OC   Acidobacteriaceae; Acidobacterium.
OX   NCBI_TaxID=240015;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 /
RC   NCIMB 13165 / 161;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-
CC       step reaction: proline is first activated by ATP to form Pro-AMP and
CC       then transferred to the acceptor end of tRNA(Pro). As ProRS can
CC       inadvertently accommodate and process non-cognate amino acids such as
CC       alanine and cysteine, to avoid such errors it has two additional
CC       distinct editing activities against alanine. One activity is designated
CC       as 'pretransfer' editing and involves the tRNA(Pro)-independent
CC       hydrolysis of activated Ala-AMP. The other activity is designated
CC       'posttransfer' editing and involves deacylation of mischarged Ala-
CC       tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
CC       {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP +
CC         diphosphate; Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC         COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC         EC=6.1.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01569};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       editing domain and the C-terminal anticodon-binding domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}.
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DR   EMBL; CP001472; ACO33322.1; -; Genomic_DNA.
DR   RefSeq; WP_015897889.1; NC_012483.1.
DR   SMR; C1F3P3; -.
DR   STRING; 240015.ACP_2832; -.
DR   KEGG; aca:ACP_2832; -.
DR   eggNOG; COG0442; Bacteria.
DR   HOGENOM; CLU_016739_0_0_0; -.
DR   InParanoid; C1F3P3; -.
DR   OMA; AACAGIY; -.
DR   OrthoDB; 9809052at2; -.
DR   CDD; cd04334; ProRS-INS; 1.
DR   CDD; cd00861; ProRS_anticodon_short; 1.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   FunFam; 3.30.930.10:FF:000065; Proline--tRNA ligase; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 2.
DR   Gene3D; 3.90.960.10; YbaK/aminoacyl-tRNA synthetase-associated domain; 1.
DR   HAMAP; MF_01569; Pro_tRNA_synth_type1; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR   InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR   InterPro; IPR050062; Pro-tRNA_synthetase.
DR   InterPro; IPR044140; ProRS_anticodon_short.
DR   InterPro; IPR033730; ProRS_core_prok.
DR   InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR   PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42753:SF2; PROLINE--TRNA LIGASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF04073; tRNA_edit; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   SUPFAM; SSF55826; YbaK/ProRS associated domain; 1.
DR   NCBIfam; NF006625; PRK09194.1; 1.
DR   NCBIfam; TIGR00409; proS_fam_II; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0002161; F:aminoacyl-tRNA deacylase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Proteomes; UP000002207; Chromosome.
DR   AlphaFoldDB; C1F3P3; -.
DR   FunCoup; C1F3P3; 533.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..585
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000185481"
SQ   SEQUENCE   585 AA;  64330 MW;  90844F150B4E2AC1 CRC64;
     MHRWSRLFVP TLREAPSDAE VASHKFLLRS GYIRQLGAGI YSYLLFGQRS INKIVGIVRE
     EMDKIGQEFL LPAIHPADLW RESGRWTVMG DNMFRLKDRK GAELCLGMTH EEVMTDIARN
     ELRSYKQLPQ IWYQIQNKFR DEPRPRSGLL RVRQFLMKDS YSFDLNQAGL DKSYDLHDAA
     YRAIFTRCGL NFVVVEADSG AMGGSGSQEF MVYTDAGEDL IASCAKCGYA ANMEKATSKL
     APVEELAATG DGQPELISTP GQAAIADICK FLGMQPHSDI KCVAYMAEVP SEDGKTSTWE
     PVAAFLRGDH FVNETKLLAV VGATELRPMQ AEELEKWMHG PAGYLGPVGL TPAKKLRDGS
     LNVVLDLGLE GRRNLVAGAN KLDYHYRNVT PGRDFTWTVA ADIRNAAEGE GCPVCGEPLK
     VAKAVEIGHI FKLGTKYTES MGARVLDENG KEVMPVMGCY GIGIERILTA SIEQNNDANG
     FWLPRSIAPF DVVVTITNMA DETLRQAGEA LAAQLEAAGY DVLLDDREER AGVKFKDADL
     VGIPYRFNVG KKTLEGKTEL VTRATASSQD VALDAAVEAL KALTA
//