ALYS_ENTFA
ID ALYS_ENTFA Reviewed; 737 AA.
AC P37710;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Autolysin;
DE EC=3.2.1.-;
DE AltName: Full=Beta-glycosidase;
DE AltName: Full=Peptidoglycan hydrolase;
DE Flags: Precursor;
GN OrderedLocusNames=EF_0799;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1679432; DOI=10.1128/jb.173.18.5619-5623.1991;
RA Beliveau C., Potvin C., Trudel J., Asselin A., Bellemare G.;
RT "Cloning, sequencing, and expression in Escherichia coli of a Streptococcus
RT faecalis autolysin.";
RL J. Bacteriol. 173:5619-5623(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
CC -!- FUNCTION: Hydrolyzes the cell wall of E.faecalis and M.lysodeikticus.
CC May play an important role in cell wall growth and cell separation.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC binding.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family. {ECO:0000305}.
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DR EMBL; M58002; AAA67325.1; -; Genomic_DNA.
DR EMBL; AE016830; AAO80613.1; -; Genomic_DNA.
DR PIR; A38109; A38109.
DR RefSeq; NP_814543.1; NC_004668.1.
DR RefSeq; WP_010706701.1; NZ_KE136527.1.
DR PDB; 2MKX; NMR; -; A=426-475.
DR PDBsum; 2MKX; -.
DR AlphaFoldDB; P37710; -.
DR BMRB; P37710; -.
DR SMR; P37710; -.
DR IntAct; P37710; 2.
DR STRING; 226185.EF_0799; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR CAZy; GH73; Glycoside Hydrolase Family 73.
DR EnsemblBacteria; AAO80613; AAO80613; EF_0799.
DR KEGG; efa:EF0799; -.
DR PATRIC; fig|226185.45.peg.2736; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG1705; Bacteria.
DR HOGENOM; CLU_013771_6_0_9; -.
DR OMA; GETVYYN; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 6.
DR Gene3D; 3.10.350.10; -; 6.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF01476; LysM; 6.
DR SMART; SM00257; LysM; 6.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF54106; SSF54106; 6.
DR PROSITE; PS51782; LYSM; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Antimicrobial; Bacteriolytic enzyme; Cell cycle;
KW Cell division; Cell wall biogenesis/degradation; Glycosidase; Hydrolase;
KW Reference proteome; Repeat; Secreted; Septation; Signal.
FT SIGNAL 1..53
FT /evidence="ECO:0000255"
FT CHAIN 54..737
FT /note="Autolysin"
FT /id="PRO_0000012115"
FT DOMAIN 361..404
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 429..472
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 497..540
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 565..608
FT /note="LysM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 631..674
FT /note="LysM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 693..736
FT /note="LysM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 85
FT /note="T -> I (in Ref. 1; AAA67325)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="A -> V (in Ref. 1; AAA67325)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="A -> T (in Ref. 1; AAA67325)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="S -> N (in Ref. 1; AAA67325)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="S -> T (in Ref. 1; AAA67325)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="A -> T (in Ref. 1; AAA67325)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="N -> S (in Ref. 1; AAA67325)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..632
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:2MKX"
FT HELIX 439..446
FT /evidence="ECO:0007829|PDB:2MKX"
FT HELIX 450..457
FT /evidence="ECO:0007829|PDB:2MKX"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:2MKX"
SQ SEQUENCE 737 AA; 77025 MW; ABB16BD506AC7507 CRC64;
MKKESMSRIE RRKAQQRKKT PVQWKKSTTL FSSALIVSSV GTPVALLPVT AEATEEQPTN
AEVAQAPTTE TGLVETPTTE TTPGTTEQPT TDSSTTTEST TESSKETPTT PSTEQPTADS
TTPVESGTTD SSVAEITPVA PSATESEAAP AVTPDDEVKV PEARVASAQT FSALSPTQSP
SEFIAELARC AQPIAQANDL YASVMMAQAI VESGWGASTL SKAPNYNLFG IKGSYNGQSV
YMDTWEYLNG KWLVKKEPFR KYPSYMESFQ DNAHVLKTTS FQAGVYYYAG AWKSNTSSYR
DATAWLTGRY ATDPSYNAKL NNVITAYNLT QYDTPSSGGN TGGGTVNPGT GGSNNQSGTN
TYYTVKSGDT LNKIAAQYGV SVANLRSWNG ISGDLIFVGQ KLIVKKGASG NTGGSGSGGS
NNNQSGTNTY YTVKSGDTLN KIAAQYGVSV ANLRSWNGIS GDLIFVGQKL IVKKGASGNT
GGSNNGGSNN NQSGTNTYYT IKSGDTLNKI AAQYGVSVAN LRSWNGISGD LIFAGQKIIV
KKGTSGNTGG SSNGGSNNNQ SGTNTYYTIK SGDTLNKISA QFGVSVANLQ AWNNISGSLI
FAGQKIIVKK GANSGSTNTN KPTNNGGGAT TSYTIKSGDT LNKISAQFGV SVANLRSWNG
IKGDLIFAGQ TIIVKKGASA GGNASSTNSA SGKRHTVKSG DSLWGLSMQY GISIQKIKQL
NGLSGDTIYI GQTLKVG
