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Database: UniProt
Entry: G5KH31_9STRE
LinkDB: G5KH31_9STRE
Original site: G5KH31_9STRE 
ID   G5KH31_9STRE            Unreviewed;       859 AA.
AC   G5KH31;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:EHJ55626.1};
DE            EC=3.5.1.28 {ECO:0000313|EMBL:EHJ55626.1};
GN   ORFNames=STRUR_1425 {ECO:0000313|EMBL:EHJ55626.1};
OS   Streptococcus urinalis 2285-97.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ55626.1, ECO:0000313|Proteomes:UP000005388};
RN   [1] {ECO:0000313|EMBL:EHJ55626.1, ECO:0000313|Proteomes:UP000005388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2285-97 {ECO:0000313|EMBL:EHJ55626.1};
RX   PubMed=24625962; DOI=10.1093/gbe/evu048;
RA   Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA   Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT   "Phylogenomics and the dynamic genome evolution of the genus
RT   Streptococcus.";
RL   Genome Biol. Evol. 6:741-753(2014).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHJ55626.1}.
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DR   EMBL; AEUZ02000001; EHJ55626.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5KH31; -.
DR   STRING; 764291.STRUR_1425; -.
DR   eggNOG; COG0860; Bacteria.
DR   Proteomes; UP000005388; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.60.40.3760; -; 5.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR013688; GBS_Bsp-like.
DR   InterPro; IPR022263; KxYKxGKxW.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   NCBIfam; TIGR03715; KxYKxGKxW; 1.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF5; SPORULATION-SPECIFIC N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF08481; GBS_Bsp-like; 5.
DR   Pfam; PF19258; KxYKxGKxW_sig; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:EHJ55626.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005388};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..859
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039645453"
FT   DOMAIN          725..853
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          37..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   859 AA;  93800 MW;  C44535B84AEC5430 CRC64;
     MKKKMYKSKK HWVIASVATV AILGTHQATI LADSSDTTMI NPTTTESSAS TPSSEQTSTI
     SSSQSDETAV TTDHSSEVTT SSEEMASVTS DSRETSTSSA ESQSQTLTDS ETANDDKVNL
     GANTVTSETA SSSAINSQTQ SFVKARVLAT SPQAQATEPV QAPVTATIEG DKTLHITYQK
     EMTAGTDVIF AVWGDQNAQN DLVWYKASDL GAAYVDLTKH REYGLYHVNT YTRTNGQMTG
     VSALTLSFPK PQVSAEVTKL SDTQFQIDVT QVPSTITAVR IPVWTSQNNQ DDLKWYQAIQ
     VASGHYQVTV NTADHHNEMG HYNIHIYGQS TITGSQVGLT VTGYDNVDTR PNAQVSIVDY
     AQDKTSFTVQ VTGTSSTKTI TKVSIAAWSE TDGQDDLKWY TPVLKNNQAS QVINIADLSN
     TTDLYRVHVY TQYSDGSQVG TNLGAYQITK PSLKTEVDTQ MTDSGINVKV TSNMVTNYQK
     VKFAVWSVVN GQDDLKWYQA DATGKAFIPF TNHKGYGDYR IDTYSFENGS HGLKSSTVTR
     NVPQDATINL KNKVTTQNYQ KSDGTIDVVV LQGENDKTIN KVRVAAWSEE KQSNLYWYTS
     SVNQSGKVVI TVNQANHYGI QGNYTIHTYL DYSDGTSSGT NLGQFLLNGP TATSASQGNY
     KAINKVIYLD AGHGGYDSGA SYYNQYEKTL NLQIQKLVQS KLQALGYTVL ATRQSDVFID
     LLDRSKEVNA TNADIFVSIH INASTSSAAN GIETYYYQYY SDYPSQINDV FDENPERLAK
     SAILANAVQS ALIANTGAQN NGVKREAFSV LRETTAPAIL AELGFISNYS EMTKLTQSAY
     QEQLANGIVS GIQKYYASI
//
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