B2HKR6 (B2HKR6_MYCMM) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
Proline--tRNA ligase HAMAP MF_01569
EC=6.1.1.15 HAMAP MF_01569

Alternative name(s):
Prolyl-tRNA synthetase HAMAP MF_01569

Gene names

Name:	proS HAMAP MF_01569 EMBL ACC40337.1
Ordered Locus Names:	MMAR_1888

Organism

Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP]

Taxonomic identifier

216594 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	582 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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. HAMAP MF_01569

Ontologies

Keywords
Biological process	Protein biosynthesis HAMAP MF_01569
Cellular component	Cytoplasm HAMAP MF_01569
Ligand	ATP-binding HAMAP MF_01569 Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase HAMAP MF_01569 EMBL ACC40337.1 Ligase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	prolyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP proline-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	B2HKR6 [UniParc]. Last modified June 10, 2008. Version 1. Checksum: 7112D967BF26D98C	FASTA	582	63,599
	10 20 30 40 50 60 MITRMSELFL RTLRDDPADA EVPSHKLLIR AGYIRPVGPG LYSWLPLGLR VLRNIERVIR 70 80 90 100 110 120 EEMNAIGGQE ILFPALLPRA PYETTNRWTE YGDGVFRLQD RRGNDYLLGP THEELFTLTV 130 140 150 160 170 180 KGEYNSYKDF PLTLYQIQIK YRDEARPRAG ILRAREFVMK DSYSFDIDSG GLKAAYHAHR 190 200 210 220 230 240 EAYQRIFDRL RVRYVIVSAV SGAMGGSASE EFLAESPVGE DTFVRCVESG YAANVEAVVT 250 260 270 280 290 300 ARPESLPIDG QPDAVVHDTG ETPTIATLVA WANEAGLGRE VSAADTLKNV LMKIRQPGGE 310 320 330 340 350 360 WELLAIGVPG DREIDEKRLA AALDPAEYVF LDDDDFGKYP FLVKGYIGPK ALRSNDVRYL 370 380 390 400 410 420 LDPRVVDGTS WITGADEPGR HVVGLVAGRD FTADGTIEAA EVREGDPAPD GAGQLVMARG 430 440 450 460 470 480 IEIGHIFQLG RKYTDAFTAD VLGEDGKPVR LTMGSYGIGV SRLVAVIAEQ HHDNLGLRWP 490 500 510 520 530 540 AEIAPFGVHL VIANKDAEAR AGAIGLASEL DGLGVEVLLD DRQASPGVKF KDAELLGMPW 550 560 570 580 VVVVGRGWAD GVVELRDRFG GQTRELTVGD SLATDIAAAI SG

References

[1]

"Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. , Mungall K., Norbertczak H., Quail M.A., Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T. Genome Res. 18:729-741(2008) [PubMed: 18403782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000854 Genomic DNA. Translation: ACC40337.1.
RefSeq	YP_001850192.1. NC_010612.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	B2HKR6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBMYCT00000035804; EBMYCP00000034244; EBMYCG00000035799.
GeneID	6226147.
GenomeReviews	Gene locus MMAR_1888 in contig CP000854_GR.
KEGG	mmi:MMAR_1888.
PATRIC	18064675. VBIMycMar75906_2022.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000016802.
HOGENOM	HBG403504.
OMA	IQPAELW.
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

B2HKR6_MYCMM

Accession

Primary (citable) accession number: B2HKR6

Entry history

Integrated into UniProtKB/TrEMBL:	June 10, 2008
Last sequence update:	June 10, 2008
Last modified:	January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)