LYTH_STAA8
ID LYTH_STAA8 Reviewed; 291 AA.
AC Q2FXU3;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 89.
DE RecName: Full=Probable cell wall amidase LytH {ECO:0000250|UniProtKB:O32421};
DE EC=3.5.1.- {ECO:0000250|UniProtKB:O32421};
DE Flags: Precursor;
GN Name=lytH; OrderedLocusNames=SAOUHSC_01739;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
RN [2]
RP PRELIMINARY FUNCTION.
RC STRAIN=ATCC 35556 / SA113;
RX PubMed=25690309; DOI=10.1007/s00253-015-6443-2;
RA Osipovitch D.C., Therrien S., Griswold K.E.;
RT "Discovery of novel S. aureus autolysins and molecular engineering to
RT enhance bacteriolytic activity.";
RL Appl. Microbiol. Biotechnol. 99:6315-6326(2015).
CC -!- FUNCTION: Probably involved in cell-wall metabolism (By similarity).
CC May have autolysin activity (PubMed:25690309).
CC {ECO:0000250|UniProtKB:O32421, ECO:0000305|PubMed:25690309}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000305}.
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DR EMBL; CP000253; ABD30811.1; -; Genomic_DNA.
DR RefSeq; WP_000717800.1; NZ_LS483365.1.
DR RefSeq; YP_500247.1; NC_007795.1.
DR AlphaFoldDB; Q2FXU3; -.
DR SMR; Q2FXU3; -.
DR STRING; 1280.SAXN108_1659; -.
DR EnsemblBacteria; ABD30811; ABD30811; SAOUHSC_01739.
DR GeneID; 3921088; -.
DR KEGG; sao:SAOUHSC_01739; -.
DR PATRIC; fig|93061.5.peg.1585; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_1_1_9; -.
DR OMA; WHTNLNI; -.
DR PRO; PR:Q2FXU3; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR InterPro; IPR017273; LytH.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR003646; SH3-like_bac-type.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF08239; SH3_3; 1.
DR PIRSF; PIRSF037730; CWA_LytH_prd; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 1.
DR PROSITE; PS51781; SH3B; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..291
FT /note="Probable cell wall amidase LytH"
FT /id="PRO_0000245426"
FT DOMAIN 41..105
FT /note="SH3b"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT DOMAIN 122..286
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000305|PubMed:25690309"
FT REGION 118..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 291 AA; 32694 MW; C296BB1178D37E1B CRC64;
MKKIEAWLSK KGLKNKRTLI VVIAFVLFII FLFLLLNSNS EDSGNITITE NAELRTGPNA
AYPVIYKVEK GDHFKKIGKV GKWIEVEDTS SNEKGWIAGW HTNLDIVADN TKEKNPLQGK
TIVLDPGHGG SDQGASSNTK YKSLEKDYTL KTAKELQRTL EKEGATVKMT RTDDTYVSLE
NRDIKGDAYL SIHNDALESS NANGMTVYWY HDNQRALADT LDATIQKKGL LSNRGSRQEN
YQVLRQTKVP AVLLELGYIS NPTDETMIKD QLHRQILEQA IVDGLKIYFS A