ID V5WCH1_9SPIO Unreviewed; 484 AA.
AC V5WCH1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01571};
DE EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01571};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01571};
DE Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01571};
GN Name=proS {ECO:0000256|HAMAP-Rule:MF_01571};
GN ORFNames=L21SP2_0037 {ECO:0000313|EMBL:AHC13483.1};
OS Salinispira pacifica.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Salinispira.
OX NCBI_TaxID=1307761 {ECO:0000313|EMBL:AHC13483.1, ECO:0000313|Proteomes:UP000018680};
RN [1] {ECO:0000313|EMBL:AHC13483.1, ECO:0000313|Proteomes:UP000018680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L21-RPul-D2 {ECO:0000313|EMBL:AHC13483.1,
RC ECO:0000313|Proteomes:UP000018680};
RX PubMed=26203324; DOI=10.1186/1944-3277-10-7;
RA Ben Hania W., Joseph M., Schumann P., Bunk B., Fiebig A., Sproer C.,
RA Klenk H.P., Fardeau M.L., Spring S.;
RT "Complete genome sequence and description of Salinispira pacifica gen.
RT nov., sp. nov., a novel spirochaete isolated form a hypersaline microbial
RT mat.";
RL Stand. Genomic Sci. 10:7-7(2015).
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_01571}.
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_01571};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01571}.
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC anticodon-binding domain and the C-terminal extension.
CC {ECO:0000256|HAMAP-Rule:MF_01571}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 3 subfamily. {ECO:0000256|HAMAP-Rule:MF_01571}.
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DR EMBL; CP006939; AHC13483.1; -; Genomic_DNA.
DR RefSeq; WP_024266416.1; NC_023035.1.
DR AlphaFoldDB; V5WCH1; -.
DR STRING; 1307761.L21SP2_0037; -.
DR KEGG; slr:L21SP2_0037; -.
DR PATRIC; fig|1307761.3.peg.37; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_001882_4_2_12; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000018680; 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; cd00862; ProRS_anticodon_zinc; 1.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR InterPro; IPR017449; Pro-tRNA_synth_II.
DR InterPro; IPR033721; ProRS_core_arch_euk.
DR NCBIfam; TIGR00408; proS_fam_I; 1.
DR PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF09180; ProRS-C_1; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SMART; SM00946; ProRS-C_1; 1.
DR SUPFAM; SSF64586; C-terminal domain of ProRS; 1.
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_01571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01571}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01571};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01571};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01571};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01571}; Reference proteome {ECO:0000313|Proteomes:UP000018680}.
FT DOMAIN 32..280
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 484 AA; 54779 MW; 425C0A62F2B9B6A9 CRC64;
MAEKITPRSE NYSDWYIDIV TQAKLADYSP VRGSMVIRPR GYAIWEKVQS ALDTMFKETG
HENAYFPLLI PEEFMRREAE HVEGFAPELA VVTHGGGQEL DEPLVIRPTS ETIIWSMYKK
WIQSYRDLPL LINQWANVMR WEKRTRLFLR TSEFLWQEGH TAHATAEEAE EETKTMLNVY
KTFAEEYMAL PVLTGVKSEN EKFAGAIDTY AIEALMQDGK ALQAGTSHFL GQNFAKAFDV
SFQNKEGKLE HVWASSWGVS TRLIGALIMA HSDDSGLVLP PRLAPTKVAV VPIFRNKTKE
QVMAYAEKIF GEIKEEVGGL PKSVILDTDE QNSPGWKFAE YEMLGVPVRV EIGPRDMENN
KVMVVRRDTK EKILMDASEA PAKIPRLLEE IQQGLFQKAK AFREENSRTA ESYDEFREIF
SGDGGKGFVT AAWNGDPAVE DRIKGETKAT IRVLPFGNEE EARGKTCIFT GEPAKHMAVF
ARAY
//
