Q9PI05 (SYA_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alanine--tRNA ligase
EC=6.1.1.7

Alternative name(s):
Alanyl-tRNA synthetase
Short name=AlaRS

Gene names

Name:	alaS
Ordered Locus Names:	Cj0506

Organism

Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]

Taxonomic identifier

192222 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter › Campylobacter jejuni › Campylobacter jejuni subsp. jejuni

Protein attributes

Sequence length	842 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain By similarity. HAMAP-Rule MF_00036
Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP-Rule MF_00036
Cofactor	Binds 1 zinc ion per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
Domain	Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs By similarity. HAMAP-Rule MF_00036
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc tRNA-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alanyl-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 alanine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW zinc ion binding Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 842	842	Alanine--tRNA ligase HAMAP-Rule MF_00036		PRO_0000075083
Sites
	Metal binding	549	1	Zinc Potential
	Metal binding	553	1	Zinc Potential
	Metal binding	650	1	Zinc Potential
	Metal binding	654	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q9PI05 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: F571EA5A2B60A8B7	FASTA	842	94,906
	10 20 30 40 50 60 MDIRKAYLDF FASKGHEITP SSPLVPDDAT LLFTNAGMVP FKSIFTGEIP RPNPPRKTSC 70 80 90 100 110 120 QTCIRAGGKH NDLDNVGYTA RHHTFFEMLG NFSFGDYFKE QAIAYAWEFV TEVLKLPKDR 130 140 150 160 170 180 LYVTVHENDD EAFNLWQKHI QKERIYKFGD KDNFWQMGDT GPCGPCSEIF YDQGQEHFNS 190 200 210 220 230 240 SEDYMGGDGD RFLEIWNLVF MQYERSADGV LSPLPKPSID TGMGLERVTA IKEGKFSNFD 250 260 270 280 290 300 SSLFMPIINE ISKLCNKTYV YESGASFRVI ADHIRSSVFL LAQGVSFDKE GRGYVLRRIL 310 320 330 340 350 360 RRALRHGYLL GFKQAFMYKL VDVVCDLMGG HYTYLNEKKD FIKEQIRLEE ERFLSTIENG 370 380 390 400 410 420 IEIFNEELKN TKEIFSGEVA FKLYDTYGFP LDLTADMLRE KNLKVDEEKF ELFMNEQKAR 430 440 450 460 470 480 AKASWKGSGD KTASGDFKNL LEKFGENHFV GYEKAECESK ILALLDEDFK EVSTLKDAGW 490 500 510 520 530 540 VMLENTPFYA TSGGQSADSG FIAKREVLDT QKFFNLNLSF IKAGEELKVN DIVHARIDTE 550 560 570 580 590 600 KREQIARHHS ATHLLHHALR EILGSHVSQA GSLVESNKLR FDFTHHKALN KEELESIEKR 610 620 630 640 650 660 VNKMIINSSE AILENMPLEE AKKSGAIALF NEKYQGNVRV LTLGESKELC GGTHVKNTAQ 670 680 690 700 710 720 IGSFYIVKES GVSAGVRRIE AVVSKAALEF VKNQLEELSK VKDELKNNDI LSGIKKLKNE 730 740 750 760 770 780 ILSLKNELKN SSKTELDSKN IQGVEICVKR IDNGDIKAMI DDFKNKFAKA VILLIQVKDE 790 800 810 820 830 840 KITLAAGVKD VPLKAGALVK EAAQILGGNG GGRDDFATAG GKDLSKINEA LKQSLETIEK AL

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL34653.1.
PIR	C81396.
RefSeq	YP_002343938.1. NC_002163.1.
3D structure databases
ProteinModelPortal	Q9PI05.
ModBase	Search...
Protein-protein interaction databases
STRING	192222.Cj0506.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL34653; CAL34653; Cj0506.
GeneID	904835.
KEGG	cje:Cj0506.
PATRIC	20057954. VBICamJej33762_0499.
Phylogenomic databases
eggNOG	COG0013.
HOGENOM	HOG000156965.
KO	K01872.
OMA	EWFDFPK.
ProtClustDB	PRK00252.
Enzyme and pathway databases
BioCyc	CJEJ192222:GJTS-491-MONOMER.
Family and domain databases
HAMAP	MF_00036_B. Ala_tRNA_synth_B.
InterPro	IPR002318. Ala-tRNA-lgiase_IIc. IPR018162. Ala-tRNA-ligase_IIc_anticod-bd. IPR018165. Ala-tRNA-synth_IIc_core. IPR018164. Ala-tRNA-synth_IIc_N. IPR023033. Ala_tRNA_ligase_euk/bac. IPR003156. Pesterase_DHHA1. IPR018163. Thr/Ala-tRNA-synth_IIc_edit. IPR012947. tRNA_SAD. [Graphical view]
PANTHER	PTHR11777:SF6. PTHR11777:SF6. 1 hit.
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
SMART	SM00863. tRNA_SAD. 1 hit. [Graphical view]
SUPFAM	SSF101353. Ala-tRNA-synth_IIc_anticod-bd. 1 hit. SSF55186. Thr/Ala-tRNA-synth_IIc_edit. 1 hit.
TIGRFAMs	TIGR00344. alaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_CAMJE

Accession

Primary (citable) accession number: Q9PI05
Secondary accession number(s): Q0PB09

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2002
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program