Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q931U5

- ATL_STAAM

UniProt

Q931U5 - ATL_STAAM

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Bifunctional autolysin

Gene

atl

Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

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.

GO - Molecular functioni

  1. amidase activity Source: InterPro
  2. mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity Source: UniProtKB-EC
  3. N-acetylmuramoyl-L-alanine amidase activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall organization Source: UniProtKB-KW
  2. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Cell wall biogenesis/degradation

Enzyme and pathway databases

BioCyciSAUR158878:GJJ5-1072-MONOMER.

Protein family/group databases

CAZyiGH73. Glycoside Hydrolase Family 73.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional autolysin
Including the following 2 domains:
N-acetylmuramoyl-L-alanine amidase (EC:3.5.1.28)
Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase (EC:3.2.1.96)
Gene namesi
Name:atl
Synonyms:nag
Ordered Locus Names:SAV1052
OrganismiStaphylococcus aureus (strain Mu50 / ATCC 700699)
Taxonomic identifieri158878 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000002481: Chromosome

Subcellular locationi

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

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2929Sequence AnalysisAdd
BLAST
Chaini30 – 12481219Bifunctional autolysinPRO_0000045474Add
BLAST

Post-translational modificationi

Undergoes proteolytic processing to generate the two extracellular lytic enzymes, probably at the septal region on the cell surface.By similarity

Interactioni

Subunit structurei

Oligomer; forms a ring structure at the cell surface which is important for efficient partitioning of daughter cells after cell division.By similarity

Protein-protein interaction databases

STRINGi158878.SAV1052.

Structurei

3D structure databases

ProteinModelPortaliQ931U5.
SMRiQ931U5. Positions 204-410, 433-576, 600-745, 935-1006, 1097-1231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati417 – 5811651Add
BLAST
Repeati588 – 7501632Add
BLAST
Repeati762 – 9241633Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni191 – 767577N-acetylmuramoyl-L-alanine amidaseBy similarityAdd
BLAST
Regioni768 – 1248481Endo-beta-N-acetylglucosaminidaseBy similarityAdd
BLAST

Domaini

The repeat domains R1, R2 and R3 are responsible for directing the proteins to the septal region.By similarity

Sequence similaritiesi

In the N-terminal section; belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.Curated
In the C-terminal section; belongs to the glycosyl hydrolase 73 family.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG4193.
HOGENOMiHOG000279968.
KOiK13714.
OMAiKSGWISK.
OrthoDBiEOG6GXTN7.

Family and domain databases

Gene3Di3.40.80.10. 1 hit.
InterProiIPR002502. Amidase_domain.
IPR013338. Lysozyme_subfam2_dom.
IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
[Graphical view]
PfamiPF01510. Amidase_2. 1 hit.
PF01832. Glucosaminidase. 1 hit.
[Graphical view]
SMARTiSM00644. Ami_2. 1 hit.
SM00047. LYZ2. 1 hit.
[Graphical view]
SUPFAMiSSF55846. SSF55846. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q931U5-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKKFNYKLP SMVALTLVGS AVTAHQVQAA ETTQDQTTNK NVLDSNKVKA
60 70 80 90 100
TTEQAKAEVK NPTQNISGTQ VYQDPAIVQP KTANNKTGNA QVSQKVDTAQ
110 120 130 140 150
VNGDTRANQS ATTNNTQPVA KSTSTTAPKT NTNVTNAGYS LVDDEDDNSE
160 170 180 190 200
HQINPELIKS AAKPAALETQ YKAAAPKAKT EATPKVTTFS ASAQPRSVAA
210 220 230 240 250
TPKTSLPKYK PQVNSSINDY IRKNNLKAPK IEEDYTSYFP KYAYRNGVGR
260 270 280 290 300
PEGIVVHDTA NDRSTINGEI SYMKNNYQNA FVHAFVDGDR IIETAPTDYL
310 320 330 340 350
SWGVGAVGNP RFINVEIVHT HDYASFARSM NNYADYAATQ LQYYGLKPDS
360 370 380 390 400
AEYDGNGTVW THYAVSKYLG GTDHADPHGY LRSHNYSYDQ LYDLINEKYL
410 420 430 440 450
IKMGKVAPWG TQFTTTPTTP SKPTTPSKPS TGKLTVAANN GVAQIKPTNS
460 470 480 490 500
GLYTTVYDKT GKATNEVQKT FAVSKTATLG NQKFYLVQDY NSGNKFGWVK
510 520 530 540 550
EGDVVYNTAK SPVNVNQSYS IKSGTKLYTV PWGTSKQVAG SVSGSGNQTF
560 570 580 590 600
KASKQQQIDK SIYLYGSVNG KSGWVSKAYL VDTAKPTPTP IPKPSTPTTN
610 620 630 640 650
NKLTVSSLNG VAQINAKNNG LFTTVYDKTG KPTKEVQKTF AVTKEASLGG
660 670 680 690 700
NKFYLVKDYN SPTLIGWVKQ GDVIYNNAKS PVNVMQTYTV KPGTKLYSVP
710 720 730 740 750
WGTYKQEAGA VSGTGNQTFK ATKQQQIDKS IYLFGTVNGK SGWVSKAYLA
760 770 780 790 800
VPAAPKKAVA QPKTAVKAYT VTKPQTTQTV SKIAQVKPNN TGIRASVYEK
810 820 830 840 850
TAKNGAKYAD RTFYVTKERA HGNETYVLLN NTSHNIPLGW FNVKDLNVQN
860 870 880 890 900
LGKEVKTTQK YTVNKSNNGL SMVPWGTKNQ VILTGNNIAQ GTFNATKQVS
910 920 930 940 950
VGKDVYLYGT INNRTGWVNA KDLTAPTAVK PTTSAAKDYN YTYVIKNGNG
960 970 980 990 1000
YYYVTPNSDT AKYSLKAFNE QPFAVVKEQV INGQTWYYGK LSNGKLAWIK
1010 1020 1030 1040 1050
STDLAKELIK YNQTGMTLNQ VAQIQAGLQY KPQVQRVPGK WTDANFNDVK
1060 1070 1080 1090 1100
HAMDTKRLAQ DPALKYQFLR LDQPQNISID KINQFLKGKG VLENQGAAFN
1110 1120 1130 1140 1150
KAAQMYGINE VYLISHALLE TGNGTSQLAK GADVVNNKVV TNSNTKYHNV
1160 1170 1180 1190 1200
FGIAAYDNDP LREGIKYAKQ AGWDTVSKAI VGGAKFIGNS YVKAGQNTLY
1210 1220 1230 1240
KMRWNPAHPG THQYATDVDW ANINAKIIKG YYDKIGEVGK YFDIPQYK
Length:1,248
Mass (Da):136,751
Last modified:July 5, 2004 - v2
Checksum:i701B54EE6152275E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB57214.2.
AJ567416 Genomic DNA. Translation: CAD98826.1.
RefSeqiNP_371576.2. NC_002758.2.

Genome annotation databases

EnsemblBacteriaiBAB57214; BAB57214; SAV1052.
GeneIDi1121029.
KEGGisav:SAV1052.
PATRICi19562801. VBIStaAur52173_1079.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000017 Genomic DNA. Translation: BAB57214.2 .
AJ567416 Genomic DNA. Translation: CAD98826.1 .
RefSeqi NP_371576.2. NC_002758.2.

3D structure databases

ProteinModelPortali Q931U5.
SMRi Q931U5. Positions 204-410, 433-576, 600-745, 935-1006, 1097-1231.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 158878.SAV1052.

Protein family/group databases

CAZyi GH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAB57214 ; BAB57214 ; SAV1052 .
GeneIDi 1121029.
KEGGi sav:SAV1052.
PATRICi 19562801. VBIStaAur52173_1079.

Phylogenomic databases

eggNOGi COG4193.
HOGENOMi HOG000279968.
KOi K13714.
OMAi KSGWISK.
OrthoDBi EOG6GXTN7.

Enzyme and pathway databases

BioCyci SAUR158878:GJJ5-1072-MONOMER.

Family and domain databases

Gene3Di 3.40.80.10. 1 hit.
InterProi IPR002502. Amidase_domain.
IPR013338. Lysozyme_subfam2_dom.
IPR002901. MGlyc_endo_b_GlcNAc_like_dom.
[Graphical view ]
Pfami PF01510. Amidase_2. 1 hit.
PF01832. Glucosaminidase. 1 hit.
[Graphical view ]
SMARTi SM00644. Ami_2. 1 hit.
SM00047. LYZ2. 1 hit.
[Graphical view ]
SUPFAMi SSF55846. SSF55846. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Mu50 / ATCC 700699.
  2. "Genetic analysis of seventeen genes in Staphylococcus aureus with reduced susceptibility to vancomycin (VRSA) and heteroVRSA (hVRSA)."
    Wootton M., Avison M.B., Bennett P.M., Howe R.A., MacGowan A.P., Walsh T.R.
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 785-1248.

Entry informationi

Entry nameiATL_STAAM
AccessioniPrimary (citable) accession number: Q931U5
Secondary accession number(s): Q7WY94, Q7WY95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: July 5, 2004
Last modified: October 29, 2014
This is version 76 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3