SYP_RHOPA
ID SYP_RHOPA Reviewed; 438 AA.
AC Q6N5P6;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Proline--tRNA ligase;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
GN Name=proS; OrderedLocusNames=RPA2928;
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=258594;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009;
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA Harrison F.H., Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
RN [2]
RP PROLINE AND CYSTEINE ACTIVATION, LACK OF EDITING ACTIVITY, AND KINETIC
RP PARAMETERS.
RX PubMed=12130657; DOI=10.1074/jbc.m206928200;
RA Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H.,
RA Hartsch T., Soell D.;
RT "Cysteine activation is an inherent in vitro property of prolyl-tRNA
RT synthetases.";
RL J. Biol. Chem. 277:34743-34748(2002).
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). Can inadvertently
CC accommodate and process cysteine. The misacylated Cys-tRNA(Pro) is not
CC edited by ProRS.
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;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.28 mM for proline {ECO:0000269|PubMed:12130657};
CC KM=0.17 mM for cysteine {ECO:0000269|PubMed:12130657};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 2 subfamily. {ECO:0000305}.
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DR EMBL; BX572602; CAE28369.1; -; Genomic_DNA.
DR RefSeq; WP_011158477.1; NC_005296.1.
DR PDB; 2I4L; X-ray; 2.00 A; A/B/C=1-438.
DR PDB; 2I4M; X-ray; 2.80 A; A/B/C=1-438.
DR PDB; 2I4N; X-ray; 2.85 A; A/B/C=1-438.
DR PDB; 2I4O; X-ray; 2.40 A; A/B/C=1-438.
DR PDBsum; 2I4L; -.
DR PDBsum; 2I4M; -.
DR PDBsum; 2I4N; -.
DR PDBsum; 2I4O; -.
DR AlphaFoldDB; Q6N5P6; -.
DR SMR; Q6N5P6; -.
DR DIP; DIP-29058N; -.
DR STRING; 258594.RPA2928; -.
DR PRIDE; Q6N5P6; -.
DR EnsemblBacteria; CAE28369; CAE28369; RPA2928.
DR GeneID; 66894011; -.
DR KEGG; rpa:RPA2928; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_016739_4_2_5; -.
DR OMA; NCDYAAN; -.
DR PhylomeDB; Q6N5P6; -.
DR BioCyc; RPAL258594:TX73_RS14935-MON; -.
DR BRENDA; 6.1.1.15; 5412.
DR SABIO-RK; Q6N5P6; -.
DR EvolutionaryTrace; Q6N5P6; -.
DR Proteomes; UP000001426; Chromosome.
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; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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 Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..438
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000248227"
FT HELIX 3..5
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 44..63
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2I4N"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 153..166
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 167..186
FT /evidence="ECO:0007829|PDB:2I4L"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2I4N"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:2I4M"
FT HELIX 244..252
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:2I4L"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:2I4L"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 275..290
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 292..296
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 312..319
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2I4L"
FT TURN 341..343
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 358..373
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 387..397
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:2I4L"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:2I4L"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 414..419
FT /evidence="ECO:0007829|PDB:2I4L"
FT TURN 420..422
FT /evidence="ECO:0007829|PDB:2I4L"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:2I4L"
FT TURN 430..434
FT /evidence="ECO:0007829|PDB:2I4L"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:2I4N"
SQ SEQUENCE 438 AA; 49309 MW; 36D07FB76904F42A CRC64;
MRLSRFFLPI LKENPKEAEI VSHRLMLRAG MLRQEAAGIY AWLPLGHRVL KKIEQIVREE
QNRAGAIELL MPTLQLADLW RESGRYDAYG PEMLRIADRH KRELLYGPTN EEMITEIFRA
YIKSYKSLPL NLYHIQWKFR DEQRPRFGVM RGREFLMKDA YSFDVDEAGA RKSYNKMFVA
YLRTFARMGL KAIPMRAETG PIGGDLSHEF IVLAETGESG VYIDRDVLNL PVPDENVDYD
GDLTPIIKQW TSVYAATEDV HEPARYESEV PEANRLNTRG IEVGQIFYFG TKYSDSMKAN
VTGPDGTDAP IHGGSYGVGV SRLLGAIIEA CHDDNGIIWP EAVAPFRVTI LNLKQGDAAT
DAACDQLYRE LSAKGVDVLY DDTDQRAGAK FATADLIGIP WQIHVGPRGL AEGKVELKRR
SDGARENLAL ADVVARLT
