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
//