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Database: UniProt
Entry: A0A437KFL7_9BACI
LinkDB: A0A437KFL7_9BACI
Original site: A0A437KFL7_9BACI 
ID   A0A437KFL7_9BACI        Unreviewed;       566 AA.
AC   A0A437KFL7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 14.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01569};
DE            EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01569};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01569};
DE            Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01569};
GN   Name=proS {ECO:0000256|HAMAP-Rule:MF_01569};
GN   ORFNames=EM808_00890 {ECO:0000313|EMBL:RVT67066.1};
OS   Niallia taxi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Niallia.
OX   NCBI_TaxID=2499688 {ECO:0000313|EMBL:RVT67066.1, ECO:0000313|Proteomes:UP000288024};
RN   [1] {ECO:0000313|EMBL:RVT67066.1, ECO:0000313|Proteomes:UP000288024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M5HDSG1-1 {ECO:0000313|EMBL:RVT67066.1,
RC   ECO:0000313|Proteomes:UP000288024};
RA   Tuo L.;
RT   "Bacillus sp. M5HDSG1-1, whole genome shotgun sequence.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01569}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC         tRNA(Pro); 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:0000256|ARBA:ARBA00000857,
CC         ECO:0000256|HAMAP-Rule:MF_01569};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC       Rule:MF_01569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01569}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RVT67066.1}.
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DR   EMBL; RZTZ01000001; RVT67066.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A437KFL7; -.
DR   Proteomes; UP000288024; Unassembled WGS sequence.
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:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd04334; ProRS-INS; 1.
DR   CDD; cd00861; ProRS_anticodon_short; 1.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
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; 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   NCBIfam; TIGR00409; proS_fam_II; 1.
DR   PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR42753:SF2; PROLYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF04073; tRNA_edit; 1.
DR   PIRSF; PIRSF001535; ProRS_1; 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   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_01569};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01569};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01569};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01569};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01569};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_01569}; Reference proteome {ECO:0000313|Proteomes:UP000288024}.
FT   DOMAIN          48..464
FT                   /note="Aminoacyl-transfer RNA synthetases class-II family
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50862"
SQ   SEQUENCE   566 AA;  63190 MW;  D5235796A0C6985F CRC64;
     MKQSKMLIPT LREVPADAEI KSHQLLLRAG YIRQNASGIY SYLPLANKVL KKIEHIIREE
     MDNSGSVELL MPALQQAELW QESGRWYSYG PELMRLNDRN DREFALGATH EEVITSLIRD
     EIKSYKRLPL SLYQIQTKFR DEKRPRFGIL RGREFIMKDA YSFHSSHESL GEVYDAIFQA
     YCNIFERCGL NFRAVIADSG AMGGKDTHEF MALSEVGEDT IAYSTDSSYA ANIEMAPVIT
     SYEKEDKPHG ALEKVKTENV KTIEQVASFL NVAENKCIKS LLFKVDESHV LVLVRGDHEV
     NDIKLKNLLE ATNVELADAA ETKTILGCSV GSLGPIGVKD VQVIADSAVQ YIVNGVCGAN
     DEDYHYINVN PDRDFAVSQY ADLRFIQEGD VSPDGKGSIV FAKGIEVGHV FKLGTRYSEA
     MGASYLDENG RSQSIIMGCY GIGVSRTMAA VVEQFNDEKG IVWPKTIAPF DLHLITVNVK
     DEAQTELTDK LYKSLKDNRY DVLVDDRAER AGVKFADSDL IGLPIRITVG KKAAEGIVEL
     KERSNGEVHE VHVDELLETI SKLLAN
//
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