Reviewed, UniProtKB/Swiss-Prot P00957 (SYA_ECOLI)

Names and origin

Protein names

Recommended name:
    Alanyl-tRNA synthetase
    EC=6.1.1.7
Alternative name(s):
    Alanine--tRNA ligase
      Short name=AlaRS

Gene names

Name:	alaS
Synonyms:	lovB
Ordered Locus Names:	b2697, JW2667

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	876 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). HAMAP MF_00036
Cofactor	Binds 1 zinc ion per subunit. HAMAP MF_00036
Subunit structure	Homotetramer. HAMAP MF_00036
Subcellular location	Cytoplasm. HAMAP MF_00036
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Domain	Zinc-finger
Ligand	ATP-binding Metal-binding Nucleotide-binding Zinc
Molecular function	Aminoacyl-tRNA synthetase Ligase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	alanyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from direct assay. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP alanine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP nucleic acid binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 876	876	Alanyl-tRNA synthetase HAMAP MF_00036		PRO_0000075113
Regions
	Zinc finger	179 – 192	14	C2H2-type HAMAP MF_00036
	Region	1 – 461	461	Catalytic HAMAP MF_00036
	Region	699 – 808	110	Important for oligomerization HAMAP MF_00036
Amino acid modifications
	Modified residue	74	1	N6-acetyllysine Ref.11
Experimental info
	Mutagenesis	179	1	C → S: Inactivates the enzyme. HAMAP MF_00036
	Mutagenesis	182	1	C → S: No inactivation. HAMAP MF_00036
	Mutagenesis	184	1	E → Q: No inactivation. HAMAP MF_00036
	Mutagenesis	188	1	D → N: No inactivation. HAMAP MF_00036
	Mutagenesis	189	1	H → Q: Inactivates the enzyme. HAMAP MF_00036
	Mutagenesis	191	1	D → N: No inactivation. HAMAP MF_00036
	Mutagenesis	192	1	H → Q: Inactivates the enzyme. HAMAP MF_00036
	Sequence conflict	29 – 33	5	LVPHN → RYHIT Ref.4
	Sequence conflict	29 – 33	5	LVPHN → RYHIT Ref.5
	Sequence conflict	158	1	G → N Ref.4
	Sequence conflict	158	1	G → N Ref.5
	Sequence conflict	168	1	D → G in AAA03208. Ref.5
	Sequence conflict	172	1	Q → R in AAA03208. Ref.5
	Sequence conflict	175	1	D → G in AAA03208. Ref.5
	Sequence conflict	180	1	G → D in AAA03208. Ref.5
	Sequence conflict	584	1	Q → H in AAA03208. Ref.5
	Sequence conflict	619	1	Q → L in AAA03208. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P00957-1 [UniParc]. Last modified November 1, 1997. Version 2. Checksum: 73F69C69FCF8C08C	FASTA	876	96,032
	10 20 30 40 50 60 MSKSTAEIRQ AFLDFFHSKG HQVVASSSLV PHNDPTLLFT NAGMNQFKDV FLGLDKRNYS 70 80 90 100 110 120 RATTSQRCVR AGGKHNDLEN VGYTARHHTF FEMLGNFSFG DYFKHDAIQF AWELLTSEKW 130 140 150 160 170 180 FALPKERLWV TVYESDDEAY EIWEKEVGIP RERIIRIGDN KGAPYASDNF WQMGDTGPCG 190 200 210 220 230 240 PCTEIFYDHG DHIWGGPPGS PEEDGDRYIE IWNIVFMQFN RQADGTMEPL PKPSVDTGMG 250 260 270 280 290 300 LERIAAVLQH VNSNYDIDLF RTLIQAVAKV TGATDLSNKS LRVIADHIRS CAFLIADGVM 310 320 330 340 350 360 PSNENRGYVL RRIIRRAVRH GNMLGAKETF FYKLVGPLID VMGSAGEDLK RQQAQVEQVL 370 380 390 400 410 420 KTEEEQFART LERGLALLDE ELAKLSGDTL DGETAFRLYD TYGFPVDLTA DVCRERNIKV 430 440 450 460 470 480 DEAGFEAAME EQRRRAREAS GFGADYNAMI RVDSASEFKG YDHLELNGKV TALFVDGKAV 490 500 510 520 530 540 DAINAGQEAV VVLDQTPFYA ESGGQVGDKG ELKGANFSFA VEDTQKYGQA IGHIGKLAAG 550 560 570 580 590 600 SLKVGDAVQA DVDEARRARI RLNHSATHLM HAALRQVLGT HVSQKGSLVN DKVLRFDFSH 610 620 630 640 650 660 NEAMKPEEIR AVEDLVNTQI RRNLPIETNI MDLEAAKAKG AMALFGEKYD ERVRVLSMGD 670 680 690 700 710 720 FSTELCGGTH ASRTGDIGLF RIISESGTAA GVRRIEAVTG EGAIATVHAD SDRLSEVAHL 730 740 750 760 770 780 LKGDSNNLAD KVRSVLERTR QLEKELQQLK EQAAAQESAN LSSKAIDVNG VKLLVSELSG 790 800 810 820 830 840 VEPKMLRTMV DDLKNQLGST IIVLATVVEG KVSLIAGVSK DVTDRVKAGE LIGMVAQQVG 850 860 870 GKGGGRPDMA QAGGTDAAAL PAALASVKGW VSAKLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Mass spectra of partial protein hydrolysates as a multiple phase check for long polypeptides deduced from DNA sequences: NH2-terminal segment of alanine tRNA synthetase." Herlihy W.C., Royal N.J., Biemann K., Putney S.D., Schimmel P.R. Proc. Natl. Acad. Sci. U.S.A. 77:6531-6535(1980) [PubMed: 7005898] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-166, PARTIAL PROTEIN SEQUENCE.
[5]	"Primary structure of a large aminoacyl-tRNA synthetase." Putney S.D., Royal N.J., de Vegvar H.N., Herlihy W.C., Biemann K., Schimmel P. Science 213:1497-1501(1981) [PubMed: 7025207] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-876.
[6]	"Acceptor helix interactions in a class II tRNA synthetase: photoaffinity cross-linking of an RNA miniduplex substrate." Musier-Forsyth K., Schimmel P. Biochemistry 33:773-779(1994) [PubMed: 8292605] [Abstract] Cited for: PROTEIN SEQUENCE OF 163-173.
[7]	"Evidence for involvement of Escherichia coli genes pmbA, csrA and a previously unrecognized gene tldD, in the control of DNA gyrase by letD (ccdB) of sex factor F." Murayama N., Shimizu H., Takiguchi S., Baba Y., Amino H., Horiuchi T., Sekimizu K., Miki T. J. Mol. Biol. 256:483-502(1996) [PubMed: 8604133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 799-876. Strain: KP4714.
[8]	"Identification and molecular characterization of csrA, a pleiotropic gene from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis, cell size, and surface properties." Romeo T., Gong M., Liu M.-Y., Brun-Zinkernagel A.-M. J. Bacteriol. 175:4744-4755(1993) [PubMed: 8393005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 866-876. Strain: K12.
[9]	"Cloning, partial sequencing, and in vitro transcription of the gene for alanine tRNA synthetase." Putney S.D., Melendez D.L., Schimmel P.R. J. Biol. Chem. 256:205-211(1981) [PubMed: 6256345] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
[10]	"Evidence for a 'cysteine-histidine box' metal-binding site in an Escherichia coli aminoacyl-tRNA synthetase." Miller W.T., Hill K.A.W., Schimmel P. Biochemistry 30:6970-6976(1991) [PubMed: 1712632] [Abstract] Cited for: ZINC-BINDING.
[11]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-74, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00096 Genomic DNA. Translation: AAC75739.1. AP009048 Genomic DNA. Translation: BAA16559.1. J01581 Unassigned DNA. Translation: AAA03208.1. L07596 Unassigned DNA. Translation: AAA71918.1. Sequence problems. D44453 Genomic DNA. Translation: BAA21554.1. Z28405 Genomic DNA. Translation: CAA82247.1.
PIR	SYECAT. E65049.
RefSeq	AP_003264.1. NP_417177.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:9080N.
2-D gel databases
SWISS-2DPAGE	P00957.
ECO2DBASE	F093.0. 6TH EDITION.
Genome annotation databases
GeneID	947175.
GenomeReviews	Gene locus JW2667 in contig AP009048_GR. Gene locus b2697 in contig U00096_GR.
KEGG	ecj:JW2667. eco:b2697.
Organism-specific databases
EchoBASE	EB0033.
EcoGene	EG10034. alaS.
CMR	Search...
Phylogenomic databases
HOGENOM	P00957.
OMA	P00957. ASGKHND.
Enzyme and pathway databases
BioCyc	EcoCyc:ALAS-MON. MetaCyc:ALAS-MON.
Family and domain databases
HAMAP	MF_00036. [Tree]
InterPro	IPR002318. Ala-tRNA-synth_IIc. IPR018165. Ala-tRNA-synth_IIc_cons-reg. IPR018164. Ala-tRNA-synth_IIc_N. IPR003156. Pesterase_DHHA1. IPR012947. tRNA_SAD. [Graphical view]
Pfam	PF02272. DHHA1. 1 hit. PF01411. tRNA-synt_2c. 1 hit. PF07973. tRNA_SAD. 1 hit. [Graphical view]
PRINTS	PR00980. TRNASYNTHALA.
TIGRFAMs	TIGR00344. alaS. 1 hit.
PROSITE	PS50860. AA_TRNA_LIGASE_II_ALA. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYA_ECOLI

Accession

Primary (citable) accession number: P00957
Secondary accession number(s): P78279

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 99 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)