SYP_PSEAE
ID SYP_PSEAE Reviewed; 571 AA.
AC Q9I502;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
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}; OrderedLocusNames=PA0956;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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=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: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; AE004091; AAG04345.1; -; Genomic_DNA.
DR PIR; C83527; C83527.
DR RefSeq; NP_249647.1; NC_002516.2.
DR RefSeq; WP_003102377.1; NZ_QZGE01000007.1.
DR PDB; 5UCM; X-ray; 2.60 A; A/B=1-571.
DR PDBsum; 5UCM; -.
DR AlphaFoldDB; Q9I502; -.
DR SMR; Q9I502; -.
DR STRING; 287.DR97_981; -.
DR PaxDb; Q9I502; -.
DR PRIDE; Q9I502; -.
DR EnsemblBacteria; AAG04345; AAG04345; PA0956.
DR GeneID; 879563; -.
DR KEGG; pae:PA0956; -.
DR PATRIC; fig|208964.12.peg.994; -.
DR PseudoCAP; PA0956; -.
DR HOGENOM; CLU_016739_0_0_6; -.
DR InParanoid; Q9I502; -.
DR OMA; NCDYAAN; -.
DR PhylomeDB; Q9I502; -.
DR BioCyc; PAER208964:G1FZ6-977-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 2.
DR Gene3D; 3.40.50.800; -; 1.
DR Gene3D; 3.90.960.10; -; 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 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; SSF55681; SSF55681; 1.
DR SUPFAM; SSF55826; SSF55826; 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..571
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000248744"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 44..63
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 77..82
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 85..88
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 153..166
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 167..187
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5UCM"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 277..287
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 304..309
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 322..329
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 349..352
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:5UCM"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 381..383
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 397..416
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 418..422
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 426..428
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 434..436
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 438..445
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 457..459
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 473..478
FT /evidence="ECO:0007829|PDB:5UCM"
FT TURN 479..482
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 486..499
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 515..524
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 535..539
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 542..549
FT /evidence="ECO:0007829|PDB:5UCM"
FT STRAND 554..557
FT /evidence="ECO:0007829|PDB:5UCM"
FT HELIX 558..568
FT /evidence="ECO:0007829|PDB:5UCM"
SQ SEQUENCE 571 AA; 63104 MW; 2380758D2523CD14 CRC64;
MRTSQYLLST LKETPADAVV ISHQLLLRAG MIRRLASGLY TWLPMGLRVL RKVETIVREE
MNAAGALEVL MPAVQPAELW QESGRWEQYG PELLRLKDRH EREFCVGPTH EEVITDLARN
ELNSYKQLPI NFYQIQTKFR DEIRPRFGLM RGREFIMKDA YSFHLSQDSL QQTYDGMYQA
YSKIFSRLGL DFRPVQADNG SIGGSGSHEF HVLANSGEDD IVFSDSSDYA ANIEKAEAVP
RESARGSATE DMRLVDTPNT KTIAALVDGF QLPIEKTIKT LVVHGAEEGT LVALIVRGDH
ELNEIKAANQ PLVASPLVFA SEAEIRAAIG AGPGSLGPVN LPIACIVDRS VALMSDFAAG
ANIEDKHYFG VNWERDLPLP EVADLRNVVE GDPSPDGKGT LVIKRGIEVG HIFQLGTKYS
EAMKLSVLSE QGKPVNLIMG CYGIGVSRVV AAAIEQNHDE RGILWPSALA PFQIALVPLK
YETESVKQAT DKLYAELTAA GFEVLLDDRD KKTSPGVKFA DMELIGIPHR IVISDRGLSE
GVLEYKGRRD SESQNLPIGE LMSFITEKLS R
