ID B9NMW5_9RHOB Unreviewed; 456 AA.
AC B9NMW5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01570};
DE EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01570};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01570};
DE Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01570};
GN Name=proS {ECO:0000256|HAMAP-Rule:MF_01570,
GN ECO:0000313|EMBL:EEE38125.1};
GN ORFNames=RKLH11_1966 {ECO:0000313|EMBL:EEE38125.1};
OS Rhodobacteraceae bacterium KLH11.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE38125.1, ECO:0000313|Proteomes:UP000005135};
RN [1] {ECO:0000313|Proteomes:UP000005135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX PubMed=21742885; DOI=10.1128/jb.05556-11;
RA Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine Lactone-
RT Producing Bacterium Isolated from the Marine Sponge Mycale laxissima.";
RL J. Bacteriol. 193:5011-5012(2011).
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). {ECO:0000256|HAMAP-
CC Rule:MF_01570}.
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_01570};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01570}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 2 subfamily. {ECO:0000256|HAMAP-Rule:MF_01570}.
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DR EMBL; DS999531; EEE38125.1; -; Genomic_DNA.
DR AlphaFoldDB; B9NMW5; -.
DR STRING; 467661.RKLH11_1966; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_016739_4_2_5; -.
DR Proteomes; UP000005135; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_01570; Pro_tRNA_synth_type2; 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; IPR023716; Prolyl-tRNA_ligase_IIa_type2.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR NCBIfam; TIGR00409; proS_fam_II; 1.
DR PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42753:SF2; PROLINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 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 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_01570};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01570};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01570};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01570};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01570};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01570}; Reference proteome {ECO:0000313|Proteomes:UP000005135}.
FT DOMAIN 43..351
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 456 AA; 51607 MW; ECF548CAFEDE37BE CRC64;
MLKFHPKGYE MRLSRYFLPV LKENPSEAQI VSHRLMLRAG MIKQAAAGIY SWLPLGFKVL
RKLENIVHEE QARAGHIAIQ MPILQSADLW RESGRYDGYG QEMLRMKDRH DRDMLFTPTA
EELVTDIFRG HVSSYKDLPL TLYQIQWKFR DEIRPRFGVM RGREFYMKDG YNFDLTMEDA
LHAYNRHLVS YLRTYERMGL QAIPMRADSG PIGGDYTHEF LVLAETGESE VFYDSAVTDL
TFGDRDIDYD NRDQCQAIMD EFTSKYARTD ETHDEALFDQ VPEDRRRVAR GIEVGQIFYF
GTNYSEAMGA TVQGPDGKPV PVHMGSHGIG VSRLIGAIIE ASHDDKGIIW PEGVTPFHCG
IVNLKQGDDE ADAACDTLYA ALTALGLEPL YDDRKERAGG KFATMDLIGL PWRITVGPRG
LKNGVVELTS RRTGESEELS PEAAVAKIAE IYKGIA
//
