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Q5HQB9

- ATL_STAEQ

UniProt

Q5HQB9 - ATL_STAEQ

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Protein

Bifunctional autolysin

Gene

atl

Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
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

BioCyciSEPI176279:GJJB-661-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
Ordered Locus Names:SERP0636
OrganismiStaphylococcus epidermidis (strain ATCC 35984 / RP62A)
Taxonomic identifieri176279 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000000531: 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 – 13351306Bifunctional autolysinPRO_0000045480Add
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

STRINGi176279.SERP0636.

Structurei

3D structure databases

ProteinModelPortaliQ5HQB9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati516 – 6811661Add
BLAST
Repeati682 – 8451642Add
BLAST
Repeati846 – 10151703Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni303 – 863561N-acetylmuramoyl-L-alanine amidaseAdd
BLAST
Regioni864 – 1335472Endo-beta-N-acetylglucosaminidaseAdd
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.

Q5HQB9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAKKFNYKLP SMVALTLFGT AFTAHQANAA EQPQNQSNHK NVLDDQTALK
60 70 80 90 100
QAEKAKSEVT QSTTNVSGTQ TYQDPTQVQP KQDTQSTTYD ASLDEMSTYN
110 120 130 140 150
EISSNQKQQS LSTDDANQNQ TNSVTKNQQE ETNDLTQEDK TSTDTNQLQE
160 170 180 190 200
TQSVAKENEK DLGANANNEQ QDKKMTASQP SENQAIETQT ASNDNESQQK
210 220 230 240 250
SQQVTSEQNE TATPKVSNTN ASGYNFDYDD EDDDSSTDHL EPISLNNVNA
260 270 280 290 300
TSKQTTSYKY KEPAQRVTTN TVKKETASNQ ATIDTKQFTP FSATAQPRTV
310 320 330 340 350
YSVSSQKTSS LPKYTPKVNS SINNYIRKKN MKAPRIEEDY TSYFPKYGYR
360 370 380 390 400
NGVGRPEGIV VHDTANDNST IDGEIAFMKR NYTNAFVHAF VDGNRIIETA
410 420 430 440 450
PTDYLSWGAG PYGNQRFINV EIVHTHDYDS FARSMNNYAD YAATQLQYYN
460 470 480 490 500
LKPDSAENDG RGTVWTHAAI SNFLGGTDHA DPHQYLRSHN YSYAELYDLI
510 520 530 540 550
YEKYLIKTKQ VAPWGTTSTK PSQPSKPSGG TNNKLTVSAN RGVAQIKPTN
560 570 580 590 600
NGLYTTVYDS KGHKTDQVQK TLSVTKTATL GNNKFYLVED YNSGKKYGWV
610 620 630 640 650
KQGDVVYNTA KAPVKVNQTY NVKAGSTLYT VPWGTPKQVA SKVSGTGNQT
660 670 680 690 700
FKATKQQQID KATYLYGTVN GKSGWISKYY LTTASKPSNP TKPSTNNQLT
710 720 730 740 750
VTNNSGVAQI NAKNSGLYTT VYDTKGKTTN QIQRTLSVTK AATLGDKKFY
760 770 780 790 800
LVGDYNTGTN YGWVKQDEVI YNTAKSPVKI NQTYNVKPGV KLHTVPWGTY
810 820 830 840 850
NQVAGTVSGK GDQTFKATKQ QQIDKATYLY GTVNGKSGWI SKYYLTAPSK
860 870 880 890 900
VQALSTQSTP APKQVKPSTQ TVNQIAQVKA NNSGIRASVY DKTAKSGTKY
910 920 930 940 950
ANRTFLINKQ RTQGNNTYVL LQDGTSNTPL GWVNINDVTT QNIGKQTQSI
960 970 980 990 1000
GKYSVKPTNN GLYSIAWGTK NQQLLAPNTL ANQAFNASKA VYVGKDLYLY
1010 1020 1030 1040 1050
GTVNNRTGWI AAKDLIQNST DAQSTPYNYT FVINNSKSYF YMDPTKANRY
1060 1070 1080 1090 1100
SLKPYYEQTF TVIKQKNING VKWYYGQLLD GKYVWIKSTD LVKEKIKYAY
1110 1120 1130 1140 1150
TGMTLNNAIN IQSRLKYKPQ VQNEPLKWSN ANYSQIKNAM DTKRLANDSS
1160 1170 1180 1190 1200
LKYQFLRLDQ PQYLSAQALN KLLKGKGVLE NQGAAFSQAA RKYGLNEIYL
1210 1220 1230 1240 1250
ISHALVETGN GTSQLAKGGD VSKGKFTTKT GHKYHNVFGI GAFDNNALVD
1260 1270 1280 1290 1300
GIKYAKNAGW TSVSKAIIGG AKFIGNSYVK AGQNTLYKMR WNPANPGTHQ
1310 1320 1330
YATDINWANV NAQVLKQFYD KIGEVGKYFE IPTYK
Length:1,335
Mass (Da):148,273
Last modified:February 15, 2005 - v1
Checksum:i0D8986BCB3DFF0A2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000029 Genomic DNA. Translation: AAW53968.1.
RefSeqiYP_188221.1. NC_002976.3.

Genome annotation databases

EnsemblBacteriaiAAW53968; AAW53968; SERP0636.
GeneIDi3241348.
KEGGiser:SERP0636.
PATRICi19612147. VBIStaEpi130894_0617.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000029 Genomic DNA. Translation: AAW53968.1 .
RefSeqi YP_188221.1. NC_002976.3.

3D structure databases

ProteinModelPortali Q5HQB9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 176279.SERP0636.

Protein family/group databases

CAZyi GH73. Glycoside Hydrolase Family 73.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAW53968 ; AAW53968 ; SERP0636 .
GeneIDi 3241348.
KEGGi ser:SERP0636.
PATRICi 19612147. VBIStaEpi130894_0617.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci SEPI176279:GJJB-661-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

  1. "Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
    Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H.
    , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
    J. Bacteriol. 187:2426-2438(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35984 / RP62A.

Entry informationi

Entry nameiATL_STAEQ
AccessioniPrimary (citable) accession number: Q5HQB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: February 15, 2005
Last modified: October 29, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3