O05814 (SYP_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proline--tRNA ligase
EC=6.1.1.15

Alternative name(s):
Prolyl-tRNA synthetase
Short name=ProRS

Gene names

Name:	proS
Ordered Locus Names:	Rv2845c, MT2911
ORF Names:	MTCY24A1.12

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS By similarity. HAMAP MF_01569
Catalytic activity	ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01569
Subunit structure	Homodimer By similarity. HAMAP MF_01569
Subcellular location	Cytoplasm By similarity HAMAP MF_01569.
Domain	Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP MF_01569
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
Sequence caution	The sequence AAK47237.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	growth Inferred from mutant phenotype. Source: MTBBASE prolyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cell wall Inferred from direct assay. Source: MTBBASE cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW proline-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 582	582	Proline--tRNA ligase HAMAP MF_01569		PRO_0000139336
Amino acid modifications
	Cross-link	173		Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup) HAMAP MF_01569

Sequences

	Sequence		Length	Mass (Da)
	O05814 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 5208D4ACBA49CDCA	FASTA	582	63,302
	10 20 30 40 50 60 MITRMSELFL RTLRDDPADA EVASHKLLIR AGYIRPVAPG LYSWLPLGLR VLRNIERVIR 70 80 90 100 110 120 DEMNAIGGQE ILFPALLPRA PYETTNRWTQ YGDSVFRLKD RRGNDYLLGP THEELFTLTV 130 140 150 160 170 180 KGEYSSYKDF PLTLYQIQTK YRDEARPRAG ILRAREFVMK DSYSFDIDAA GLKAAYHAHR 190 200 210 220 230 240 EAYQRIFDRL QVRYVIVSAV SGAMGGSASE EFLAESPSGE DAFVRCLESG YAANVEAVVT 250 260 270 280 290 300 ARPDTLPIDG LPEAVVHDTG DTPTIASLVA WANEADLGRT VTAADTLKNV LIKVRQPGGD 310 320 330 340 350 360 TELLAIGVPG DREVDDKRLG AALEPADYAL LDDDDFAKHP FLVKGYIGPK ALRENNVRYL 370 380 390 400 410 420 VDPRIVDGTS WITGADQPGR HVVGLVAGRD FTADGTIEAA EVREGDPSPD GAGPLVMARG 430 440 450 460 470 480 IEIGHIFQLG SKYTDAFTAD VLGEDGKPVR LTMGSYGIGV SRLVAVVAEQ HHDELGLRWP 490 500 510 520 530 540 STVAPFDVHL VIANKDAQAR AGATALAADL DRLGVEVLLD DRQASPGVKF KDAELLGMPW 550 560 570 580 IVVVGRGWAD GVVELRDRFS GQTRELVAGA SLATDIAAAV TG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis." Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H. PLoS ONE 5:E8589-E8589(2010) [PubMed: 20066036] [Abstract] Cited for: PUPYLATION AT LYS-173, IDENTIFICATION BY MASS SPECTROMETRY. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX842581 Genomic DNA. Translation: CAB08445.1. AE000516 Genomic DNA. Translation: AAK47237.1. Different initiation.
PIR	H70588.
RefSeq	NP_217361.1. NC_000962.2. NP_337423.2. NC_002755.2.
3D structure databases
ProteinModelPortal	O05814.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000002624; EBMYCP00000002624; EBMYCG00000002622. EBMYCT00000069288; EBMYCP00000067347; EBMYCG00000069283.
GeneID	888539. 925364.
GenomeReviews	Gene locus MT2911 in contig AE000516_GR. Gene locus Rv2845c in contig AL123456_GR.
KEGG	mtc:MT2911. mtu:Rv2845c.
PATRIC	18128174. VBIMycTub22151_3186.
TIGR	MT2911.
Organism-specific databases
TubercuList	Rv2845c.
Phylogenomic databases
GeneTree	EBGT00050000016802.
HOGENOM	HBG403504.
OMA	IQPAELW.
PhylomeDB	O05814.
ProtClustDB	PRK09194.
Family and domain databases
HAMAP	MF_01569. Pro_tRNA_synth_type1. [Tree]
InterPro	IPR002314. aa-tRNA-synt_IIb_cons-dom. IPR006195. aa-tRNA-synth_II. IPR004154. Anticodon-bd. IPR002316. Pro-tRNA-synth_IIa. IPR004500. Pro-tRNA-synth_IIa_bac-type. IPR023717. Pro-tRNA-Synthase_IIa_type1. IPR007214. YbaK/aa-tRNA-synth-assoc-dom. [Graphical view]
Gene3D	G3DSA:3.40.50.800. Anticodon_bd. 1 hit. G3DSA:3.90.960.10. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
KO	K01881.
PANTHER	PTHR11451:SF3. PTHR11451:SF3. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF04073. YbaK. 1 hit. [Graphical view]
PRINTS	PR01046. TRNASYNTHPRO.
SUPFAM	SSF52954. Anticodon_bd. 1 hit. SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMs	TIGR00409. ProS_fam_II. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYP_MYCTU

Accession

Primary (citable) accession number: O05814

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program