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Database: UniProt
Entry: LYTH_STAS1
LinkDB: LYTH_STAS1
Original site: LYTH_STAS1 
ID   LYTH_STAS1              Reviewed;         291 AA.
AC   Q49Y70;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=Probable cell wall amidase LytH;
DE            EC=3.5.1.-;
DE   Flags: Precursor;
GN   Name=lytH; OrderedLocusNames=SSP1127;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
CC   -!- FUNCTION: Probably involved in cell-wall metabolism. {ECO:0000250}.
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; AP008934; BAE18272.1; -; Genomic_DNA.
DR   RefSeq; WP_011302955.1; NZ_MTGA01000038.1.
DR   AlphaFoldDB; Q49Y70; -.
DR   SMR; Q49Y70; -.
DR   KEGG; ssp:SSP1127; -.
DR   PATRIC; fig|342451.11.peg.1127; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_1_1_9; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000006371; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR017273; LytH.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
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   SUPFAM; SSF53187; Zn-dependent exopeptidases; 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_0000226289"
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:0000255"
FT   REGION          109..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32627 MW;  429A97F588CF3796 CRC64;
     MKKFNDWLEK HNLRNIPTLI VVVAFVLFVF MTIAFLNHND EDSSTIYITE DAELRTGPSA
     AYPEIHSIDK GQNFHKIGKT GKWIEVVSSN NKEKGWVAGW HTNLNIQADK NPNAKPLKDK
     TIVLDPGHGG SDQGASSNTH KKSKEKVYTL KTAKELKALL EKEGATVSMT RESDTYVTLD
     DRNIKGDAYI SIHNDSLKSS KANGSTVYWF KDNQKALAET LSASLQKKAL LTNKGARQEN
     FQVLRQTNVP AVLLELGYIS NPTDEDMITE KLHRHIVEQA IVEGLRAYFS E
//
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