Q99V41 (ATL_STAAN) 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
Ordered Locus Names:	SA0905

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	1248 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 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 – 29	29	Potential
	Chain	30 – 1248	1219	Bifunctional autolysin		PRO_0000045475
Regions
	Repeat	417 – 581	165	1
	Repeat	588 – 750	163	2
	Repeat	762 – 924	163	3
	Region	191 – 767	577	N-acetylmuramoyl-L-alanine amidase
	Region	768 – 1248	481	Endo-beta-N-acetylglucosaminidase

Sequences

	Sequence		Length	Mass (Da)
	Q99V41 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 701B54EE6152275E	FASTA	1,248	136,751
	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 HQINPELIKS AAKPAALETQ YKAAAPKAKT 190 200 210 220 230 240 EATPKVTTFS ASAQPRSVAA TPKTSLPKYK PQVNSSINDY IRKNNLKAPK IEEDYTSYFP 250 260 270 280 290 300 KYAYRNGVGR PEGIVVHDTA NDRSTINGEI SYMKNNYQNA FVHAFVDGDR IIETAPTDYL 310 320 330 340 350 360 SWGVGAVGNP RFINVEIVHT HDYASFARSM NNYADYAATQ LQYYGLKPDS AEYDGNGTVW 370 380 390 400 410 420 THYAVSKYLG GTDHADPHGY LRSHNYSYDQ LYDLINEKYL IKMGKVAPWG TQFTTTPTTP 430 440 450 460 470 480 SKPTTPSKPS TGKLTVAANN GVAQIKPTNS GLYTTVYDKT GKATNEVQKT FAVSKTATLG 490 500 510 520 530 540 NQKFYLVQDY NSGNKFGWVK EGDVVYNTAK SPVNVNQSYS IKSGTKLYTV PWGTSKQVAG 550 560 570 580 590 600 SVSGSGNQTF KASKQQQIDK SIYLYGSVNG KSGWVSKAYL VDTAKPTPTP IPKPSTPTTN 610 620 630 640 650 660 NKLTVSSLNG VAQINAKNNG LFTTVYDKTG KPTKEVQKTF AVTKEASLGG NKFYLVKDYN 670 680 690 700 710 720 SPTLIGWVKQ GDVIYNNAKS PVNVMQTYTV KPGTKLYSVP WGTYKQEAGA VSGTGNQTFK 730 740 750 760 770 780 ATKQQQIDKS IYLFGTVNGK SGWVSKAYLA VPAAPKKAVA QPKTAVKAYT VTKPQTTQTV 790 800 810 820 830 840 SKIAQVKPNN TGIRASVYEK TAKNGAKYAD RTFYVTKERA HGNETYVLLN NTSHNIPLGW 850 860 870 880 890 900 FNVKDLNVQN LGKEVKTTQK YTVNKSNNGL SMVPWGTKNQ VILTGNNIAQ GTFNATKQVS 910 920 930 940 950 960 VGKDVYLYGT INNRTGWVNA KDLTAPTAVK PTTSAAKDYN YTYVIKNGNG YYYVTPNSDT 970 980 990 1000 1010 1020 AKYSLKAFNE QPFAVVKEQV INGQTWYYGK LSNGKLAWIK STDLAKELIK YNQTGMTLNQ 1030 1040 1050 1060 1070 1080 VAQIQAGLQY KPQVQRVPGK WTDANFNDVK HAMDTKRLAQ DPALKYQFLR LDQPQNISID 1090 1100 1110 1120 1130 1140 KINQFLKGKG VLENQGAAFN KAAQMYGINE VYLISHALLE TGNGTSQLAK GADVVNNKVV 1150 1160 1170 1180 1190 1200 TNSNTKYHNV FGIAAYDNDP LREGIKYAKQ AGWDTVSKAI VGGAKFIGNS YVKAGQNTLY 1210 1220 1230 1240 KMRWNPAHPG THQYATDVDW ANINAKIIKG YYDKIGEVGK YFDIPQYK

References

[1]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: N315.

[2]

"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315." Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F. Submitted (OCT-2007) to UniProtKB Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Strain: N315.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000018 Genomic DNA. Translation: BAB42150.1.
PIR	C89874.
RefSeq	NP_374172.1. NC_002745.2.
3D structure databases
ProteinModelPortal	Q99V41.
SMR	Q99V41. Positions 204-410, 433-576, 600-745, 935-1006, 1097-1231.
ModBase	Search...
Protein-protein interaction databases
STRING	158879.SA0905.
Protein family/group databases
CAZy	GH73. Glycoside Hydrolase Family 73.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	BAB42150; BAB42150; BAB42150.
GeneID	1123728.
KEGG	sau:SA0905.
PATRIC	19573994. VBIStaAur116463_0967.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG4193.
HOGENOM	HOG000279968.
KO	K13714.
OMA	KSGWISK.
ProtClustDB	CLSK886177.
Enzyme and pathway databases
BioCyc	SAUR158879:GJCB-957-MONOMER.
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_STAAN

Accession

Primary (citable) accession number: Q99V41

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 10, 2006
Last sequence update:	June 1, 2001
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