Reviewed, UniProtKB/Swiss-Prot Q2FZK7 (ATL_STAA8)

Names and origin

Protein names

Recommended name:
    Bifunctional autolysin
Including the following 2 domains:
    1- Recommended name:
            N-acetylmuramoyl-L-alanine amidase
              EC=3.5.1.28
    2- Recommended name:
            Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
              EC=3.2.1.96

Gene names

Name:	atl
Synonyms:	nag
Ordered Locus Names:	SAOUHSC_00994

Organism

Staphylococcus aureus (strain NCTC 8325) [Complete proteome] [HAMAP]

Taxonomic identifier

93061 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	1256 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Endohydrolysis of the di-N-acetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -[(Man)5(GlcNAc)2]-Asn structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact. Cleaves the peptidoglycan connecting the daughter cells at the end of the cell division cycle, resulting in the separation of the two newly divided cells. Acts as an autolysin in penicillin-induced lysis By similarity.
Catalytic activity	Hydrolyzes the link between N-acetylmuramoyl residues and L-amino acid residues in certain cell-wall glycopeptides. Endohydrolysis of the N,N'-diacetylchitobiosyl unit in high-mannose glycopeptides and glycoproteins containing the -(Man(GlcNAc)2)Asn-structure. One N-acetyl-D-glucosamine residue remains attached to the protein; the rest of the oligosaccharide is released intact.
Subunit structure	Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division By similarity.
Subcellular location	Secreted By similarity. Note: Secreted, and then anchored on the cell surface at the peripheral cell wall above the completed septum (septal region), for the next cell division cycle By similarity.
Domain	The repeat domains R1, R2 and R3 are responsible for directing the proteins to the septal region By similarity.
Post-translational modification	Undergoes proteolytic processing to generate the two extracellular lytic enzymes, probably at the septal region on the cell surface By similarity.
Sequence similarities	In the N-terminal section; belongs to the N-acetylmuramoyl-L-alanine amidase 2 family. In the C-terminal section; belongs to the glycosyl hydrolase 73 family.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Repeat Signal
Molecular function	Hydrolase
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	cellular cell wall macromolecule metabolic process Inferred from electronic annotation. Source: InterPro cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	N-acetylmuramoyl-L-alanine amidase activity Inferred from electronic annotation. Source: EC amidase activity Inferred from electronic annotation. Source: InterPro mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase 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
	Signal peptide	1 – 29	29	Potential
	Chain	30 – 1256	1227	Bifunctional autolysin		PRO_0000247668
Regions
	Repeat	425 – 589	165	1
	Repeat	596 – 758	163	2
	Repeat	770 – 932	163	3
	Region	199 – 775	577	N-acetylmuramoyl-L-alanine amidase
	Region	776 – 1256	481	Endo-beta-N-acetylglucosaminidase

Sequences

	Sequence		Length	Mass (Da)
	Q2FZK7-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 2BB76CAA292FDD20	FASTA	1,256	137,384
	10 20 30 40 50 60 MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA TTEQAKAEVK 70 80 90 100 110 120 NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ VNGDTRANQS ATTNNTQPVA 130 140 150 160 170 180 KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE NQINPELIKS AAKPAALETQ YKTAAPKAAT 190 200 210 220 230 240 TSAPKAKTEA TPKVTTFSAS AQPRSVAATP KTSLPKYKPQ VNSSINDYIC KNNLKAPKIE 250 260 270 280 290 300 EDYTSYFPKY AYRNGVGRPE GIVVHDTAND RSTINGEISY MKNNYQNAFV HAFVDGDRII 310 320 330 340 350 360 ETAPTDYLSW GVGAVGNPRF INVEIVHTHD YASFARSMNN YADYAATQLQ YYGLKPDSAE 370 380 390 400 410 420 YDGNGTVWTH YAVSKYLGGT DHADPHGYLR SHNYSYDQLY DLINEKYLIK MGKVAPWGTQ 430 440 450 460 470 480 STTTPTTPSK PTTPSKPSTG KLTVAANNGV AQIKPTNSGL YTTVYDKTGK ATNEVQKTFA 490 500 510 520 530 540 VSKTATLGNQ KFYLVQDYNS GNKFGWVKEG DVVYNTAKSP VNVNQSYSIK PGTKLYTVPW 550 560 570 580 590 600 GTSKQVAGSV SGSGNQTFKA SKQQQIDKSI YLYGSVNGKS GWVSKAYLVD TAKPTPTPTP 610 620 630 640 650 660 KPSTPTTNNK LTVSSLNGVA QINAKNNGLF TTVYDKTGKP TKEVQKTFAV TKEASLGGNK 670 680 690 700 710 720 FYLVKDYNSP TLIGWVKQGD VIYNNAKSPV NVMQTYTVKP GTKLYSVPWG TYKQEAGAVS 730 740 750 760 770 780 GTGNQTFKAT KQQQIDKSIY LFGTVNGKSG WVSKAYLAVP AAPKKAVAQP KTAVKAYTVT 790 800 810 820 830 840 KPQTTQTVSK IAQVKPNNTG IRASVYEKTA KNGAKYADRT FYVTKERAHG NETYVLLNNT 850 860 870 880 890 900 SHNIPLGWFN VKDLNVQNLG KEVKTTQKYT VNKSNNGLSM VPWGTKNQVI LTGNNIAQGT 910 920 930 940 950 960 FNATKQVSVG KDVYLYGTIN NRTGWVNAKD LTAPTAVKPT TSAAKDYNYT YVIKNGNGYY 970 980 990 1000 1010 1020 YVTPNSDTAK YSLKAFNEQP FAVVKEQVIN GQTWYYGKLS NGKLAWIKST DLAKELIKYN 1030 1040 1050 1060 1070 1080 QTGMTLNQVA QIQAGLQYKP QVQRVPGKWT DAKFNDVKHA MDTKRLAQDP ALKYQFLRLD 1090 1100 1110 1120 1130 1140 QPQNISIDKI NQFLKGKGVL ENQGAAFNKA AQMYGINEVY LISHALLETG NGTSQLAKGA 1150 1160 1170 1180 1190 1200 DVVNNKVVTN SNTKYHNVFG IAAYDNDPLR EGIKYAKQAG WDTVSKAIVG GAKFIGNSYV 1210 1220 1230 1240 1250 KAGQNTLYKM RWNPAHPGTH QYATDVDWAN INAKIIKGYY DKIGEVGKYF DIPQYK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A Staphylococcus aureus autolysin that has an N-acetylmuramoyl-L-alanine amidase domain and an endo-beta-N-acetylglucosaminidase domain: cloning, sequence analysis, and characterization." Oshida T., Sugai M., Komatsuzawa H., Hong Y.-M., Suginaka H., Tomasz A. Proc. Natl. Acad. Sci. U.S.A. 92:285-289(1995) [PubMed: 7816834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 205-214 AND 776-792.
[2]	Foster S.J. Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The Staphylococcus aureus NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	D17366 Genomic DNA. Translation: BAA04185.1. L41499 Genomic DNA. Translation: AAA99982.1. CP000253 Genomic DNA. Translation: ABD30118.1.
RefSeq	YP_499546.1.
3D structure databases
SMR	Q2FZK7. Positions 238-391.
ModBase	Search...
Protein-protein interaction databases
STRING	Q2FZK7.
Protein family/group databases
CAZy	GH73. Glycoside Hydrolase Family 73.
Genome annotation databases
GeneID	3920394.
GenomeReviews	Gene locus SAOUHSC_00994 in contig CP000253_GR.
KEGG	sao:SAOUHSC_00994.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG5632.
HOGENOM	HBG692910.
OMA	KSGWISK.
Enzyme and pathway databases
BioCyc	SAUR93061:SAOUHSC_00994-MONOMER.
Family and domain databases
InterPro	IPR002502. Amidase_2. IPR013338. Lysozyme_dom_subfam2. IPR002901. Mano_Glyc_endo_b_GlcNAc. [Graphical view]
Pfam	PF01510. Amidase_2. 1 hit. PF01832. Glucosaminidase. 1 hit. [Graphical view]
SMART	SM00644. Ami_2. 1 hit. SM00047. LYZ2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ATL_STAA8

Accession

Primary (citable) accession number: Q2FZK7
Secondary accession number(s): O32391 , P52081, Q7WTC6, Q7WY94, Q7WY95

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	March 21, 2006
Last modified:	January 19, 2010
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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