P0C5Z8 (ATL_STAAU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional autolysin

Including the following 2 domains:

1. N-acetylmuramoyl-L-alanine amidase
   EC=3.5.1.28
2. Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
   EC=3.2.1.96

Gene names

Name:	atl
Synonyms:	nag

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus

Protein attributes

Sequence length	1255 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. Ref.3
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. Ref.4
Subcellular location	Secreted. 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. Ref.4 Ref.5 Ref.6
Domain	The repeat domains R1, R2 and R3 are responsible for directing the proteins to the septal region.
Post-translational modification	Undergoes proteolytic processing to generate the two extracellular lytic enzymes, probably at the septal region on the cell surface.
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.
Sequence caution	The sequence AAP44166.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Cell wall biogenesis/degradation
Cellular component	Secreted
Domain	Repeat Signal
Molecular function	Hydrolase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological_process	cell wall macromolecule metabolic process Inferred from electronic annotation. Source: InterPro 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 – 36	36	Potential
	Chain	37 – 1255	1219	Bifunctional autolysin		PRO_0000012114
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 – 1255	480	Endo-beta-N-acetylglucosaminidase
Experimental info
	Sequence conflict	932	1	A → R in BAA22600. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P0C5Z8 [UniParc]. Last modified January 15, 2008. Version 1. Checksum: 7257DD87168AAE7D	FASTA	1,255	137,535
	10 20 30 40 50 60 MLGVINRMAK KFNYKLPSMV ALTLVGSAVT AHQVQAAETT QDQTTNKNVL DSNKVKATTE 70 80 90 100 110 120 QAKAEVKNPT QNISGTQVYQ DPAIVQPKTA NNKTGNAQVS QKVDTAQVNG DTRANQSATT 130 140 150 160 170 180 NNTQPVAKST STTAPKTNTN VTNAGYSLVD DEDDNSEHQI NPELIKSAAK PAALETQYKA 190 200 210 220 230 240 AAPKAKTEAT PKVTTFSASA QPRSVAATPK TSLPKYKPQV NSSINDYIRK NNLKAPKIEE 250 260 270 280 290 300 DYTSYFPKYA YRNGVGRPEG IVVHDTANDR STINGEISYM KNNYQNAFVH AFVDGDRIIE 310 320 330 340 350 360 TAPTDYLSWG VGAVGNPRFI NVEIVHTHDY ASFARSMNNY ADYAATQLQY YGLKPDSAEY 370 380 390 400 410 420 DGNGTVWTHY AVSKYLGGTD HADPHGYLRS HNYSYDQLYD LINEKYLIKM GKVAPWGTQF 430 440 450 460 470 480 TTTPTTPSKP TTPSKPSTGK LTVAANNGVA QIKPTNSGLY TTVYDKTGKA TNEVQKTFAV 490 500 510 520 530 540 SKTATLGNQK FYLVQDYNSG NKFGWVKEGD VVYNTAKSPV NVNQSYSIKS GTKLYTVPWG 550 560 570 580 590 600 TSKQVAGSVS GSGNQTFKAS KQQQIDKSIY LYGSVNGKSG WVSKAYLVDT AKPTPTPIPK 610 620 630 640 650 660 PSTPTTNNKL TVSSLNGVAQ INAKNNGLFT TVYDKTGKPT KEVQKTFAVT KEASLGGNKF 670 680 690 700 710 720 YLVKDYNSPT LIGWVKQGDV IYNNAKSPVN VMQTYTVKPG TKLYSVPWGT YKQEAGAVSG 730 740 750 760 770 780 TGNQTFKATK QQQIDKSIYL FGTVNGKSGW VSKAYLAVPA APKKAVAQPK TAVKAYTVTK 790 800 810 820 830 840 PQTTQTVSKI AQVKPNNTGI RASVYEKTAK NGAKYADRTF YVTKERAHGN ETYVLLNNTS 850 860 870 880 890 900 HNIPLGWFNV KDLNVQNLGK EVKTTQKYTV NKSNNGLSMV PWGTKNQVIL TGNNIAQGTF 910 920 930 940 950 960 NATKQVSVGK DVYLYGTINN RTGWVNAKDL TAPTAVKPTT SAAKDYNYTY VIKNGNGYYY 970 980 990 1000 1010 1020 VTPNSDTAKY SLKAFNEQPF AVVKEQVING QTWYYGKLSN GKLAWIKSTD LAKELIKYNQ 1030 1040 1050 1060 1070 1080 TGMTLNQVAQ IQAGLQYKPQ VQRVPGKWTD ANFNDVKHAM DTKRLAQDPA LKYQFLRLDQ 1090 1100 1110 1120 1130 1140 PQNISIDKIN QFLKGKGVLE NQGAAFNKAA QMYGINEVYL ISHALLETGN GTSQLAKGAD 1150 1160 1170 1180 1190 1200 VVNNKVVTNS NTKYHNVFGI AAYDNDPLRE GIKYAKQAGW DTVSKAIVGG AKFIGNSYVK 1210 1220 1230 1240 1250 AGQNTLYKMR WNPAHPGTHQ YATDVDWANI NAKIIKGYYD KIGEVGKYFD IPQYK

References

[1]	"Resistance to autolysis in vancomycin-selected Staphylococcus aureus isolates precedes vancomycin-intermediate resistance." Boyle-Vavra S., Challapalli M., Daum R.S. Antimicrob. Agents Chemother. 47:2036-2039(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: IL-A.
[2]	"Novel cytotoxin in a clinical isolate of methicillin-resistant S. aureus: cloning, sequencing and expression." Kamitani S., Minamide W., Yutsudo T., Noda M. Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1255.
[3]	"Identification of endo-beta-N-acetylglucosaminidase and N-acetylmuramyl-L-alanine amidase as cluster-dispersing enzymes in Staphylococcus aureus." Sugai M., Komatsuzawa H., Akiyama T., Hong Y.-M., Oshida T., Miyake Y., Yamaguchi T., Suginaka H. J. Bacteriol. 177:1491-1496(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
[4]	"An autolysin ring associated with cell separation of Staphylococcus aureus." Yamada S., Sugai M., Komatsuzawa H., Nakashima S., Oshida T., Matsumoto A., Suginaka H. J. Bacteriol. 178:1565-1571(1996) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, SUBUNIT. Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
[5]	"Subcellular localization of the major autolysin, ATL and its processed proteins in Staphylococcus aureus." Komatsuzawa H., Sugai M., Nakashima S., Yamada S., Matsumoto A., Oshida T., Suginaka H. Microbiol. Immunol. 41:469-479(1997) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
[6]	"Localized perforation of the cell wall by a major autolysin: atl gene products and the onset of penicillin-induced lysis of Staphylococcus aureus." Sugai M., Yamada S., Nakashima S., Komatsuzawa H., Matsumoto A., Oshida T., Suginaka H. J. Bacteriol. 179:2958-2962(1997) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. Strain: ATCC 6538P / FDA 209P / DSM 346 / NCIMB 8625 / NCTC 7447.
[7]	"Targeting of muralytic enzymes to the cell division site of Gram-positive bacteria: repeat domains direct autolysin to the equatorial surface ring of Staphylococcus aureus." Baba T., Schneewind O. EMBO J. 17:4639-4646(1998) [PubMed] [Europe PMC] [Abstract] Cited for: ROLE OF REPEATS IN LOCALIZATION AT THE SEPTAL REGION. Strain: OS2.
[8]	"Modification of autolysis by synthetic peptides derived from the presumptive binding domain of Staphylococcus aureus autolysin." Takano M., Oshida T., Yasojima A., Yamada M., Okagaki C., Sugai M., Suginaka H., Matsushita T. Microbiol. Immunol. 44:463-472(2000) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING TO THE BACTERIAL CELL WALL.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF537210 Genomic DNA. Translation: AAP44166.1. Different initiation. D42078 Genomic DNA. Translation: BAA22600.1.
3D structure databases
ProteinModelPortal	P0C5Z8.
ModBase	Search...
Protein family/group databases
CAZy	GH73. Glycoside Hydrolase Family 73.
Proteomic databases
PRIDE	P0C5Z8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	COG4193.
Family and domain databases
Gene3D	3.40.80.10. 1 hit.
InterPro	IPR002502. Amidase_domain. 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]
SUPFAM	SSF55846. Amidase_2. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ATL_STAAU

Accession

Primary (citable) accession number: P0C5Z8
Secondary accession number(s): O32391 , P0C1R4, P52081, Q7WTC6, Q7WY94, Q7WY95

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program