SYP2_BACAN
ID SYP2_BACAN Reviewed; 508 AA.
AC Q81Z76; Q6I418; Q6KXS9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Proline--tRNA ligase 2 {ECO:0000255|HAMAP-Rule:MF_01571};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571};
DE AltName: Full=Prolyl-tRNA synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01571};
DE Short=ProRS 2 {ECO:0000255|HAMAP-Rule:MF_01571};
GN Name=proS2 {ECO:0000255|HAMAP-Rule:MF_01571};
GN OrderedLocusNames=BA_0396, GBAA_0396, BAS0382;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
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:0000255|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:0000255|HAMAP-Rule:MF_01571};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01571}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571}.
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DR EMBL; AE016879; AAP24426.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT52713.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29491.1; -; Genomic_DNA.
DR RefSeq; NP_842940.1; NC_003997.3.
DR RefSeq; WP_003172446.1; NZ_WXXJ01000026.1.
DR RefSeq; YP_026662.1; NC_005945.1.
DR AlphaFoldDB; Q81Z76; -.
DR SMR; Q81Z76; -.
DR IntAct; Q81Z76; 1.
DR STRING; 261594.GBAA_0396; -.
DR DNASU; 1086703; -.
DR EnsemblBacteria; AAP24426; AAP24426; BA_0396.
DR EnsemblBacteria; AAT29491; AAT29491; GBAA_0396.
DR GeneID; 45020455; -.
DR KEGG; ban:BA_0396; -.
DR KEGG; bar:GBAA_0396; -.
DR KEGG; bat:BAS0382; -.
DR PATRIC; fig|198094.11.peg.391; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_001882_4_2_9; -.
DR OMA; EVYWVTH; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 3.30.110.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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 PANTHER; PTHR43382; PTHR43382; 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; SSF55681; SSF55681; 1.
DR SUPFAM; SSF64586; SSF64586; 1.
DR TIGRFAMs; TIGR00408; proS_fam_I; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..508
FT /note="Proline--tRNA ligase 2"
FT /id="PRO_0000249116"
SQ SEQUENCE 508 AA; 58478 MW; DA4B38B4788E5131 CRC64;
MAKEQVQAIT KMEEDFAQWY TDIVKKAELV DYSSVKGCMI LRPYGYALWE NMQKVMDEKL
KATGHENVYM PMFIPESLLQ KEKDHVEGFA PEVAWVTHGG DEKLAERLCV RPTSETLFCE
HFSKIVQSYN DLPKLYNQWC SVVRWEKTTR PFLRTTEFLW QEGHTIHETA EESQAETLNI
LNLYASFCED YLAIPVIKGQ KTEKEKFAGA KATYTIESLM HDGKALQTGT SHNFGTNFSE
AFDIKFLDRN GKWQYVHQTS WGVSTRMIGG LIMVHSDNNG LVMPPKVAPV QVVIVPIAQH
KEGVLAKATE LQGHIQKVAR VKIDASNKTP GWKFNEYEMK GIPIRLEVGP KDIEKNQVVL
VRRDTKEKEF ISMDQLEERI PALLEEIHNS LFNKAKVFRD ENTYSVTNFE EMKKLADEKQ
GFIKAMWCGE LACEEKLKEE VASRCMPFEQ EHLAEECVCC VNKWCIGEKR INALLDRKDE
KDFGLHNKCN PKSFLVLQFV SCIFKMEG
