ID A0A0B5ASG7_9BACL Unreviewed; 512 AA.
AC A0A0B5ASG7;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:AJD91622.1};
DE EC=3.5.1.28 {ECO:0000313|EMBL:AJD91622.1};
GN ORFNames=JMA_23050 {ECO:0000313|EMBL:AJD91622.1};
OS Jeotgalibacillus malaysiensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Jeotgalibacillus.
OX NCBI_TaxID=1508404 {ECO:0000313|EMBL:AJD91622.1, ECO:0000313|Proteomes:UP000031449};
RN [1] {ECO:0000313|EMBL:AJD91622.1, ECO:0000313|Proteomes:UP000031449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D5 {ECO:0000313|EMBL:AJD91622.1,
RC ECO:0000313|Proteomes:UP000031449};
RA Yaakop A.S., Chan K.-G., Goh K.M.;
RT "Complete genome of a marine bacteria Jeotgalibacillus malaysiensis.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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DR EMBL; CP009416; AJD91622.1; -; Genomic_DNA.
DR RefSeq; WP_052268687.1; NZ_CP009416.1.
DR AlphaFoldDB; A0A0B5ASG7; -.
DR STRING; 1508404.JMA_23050; -.
DR KEGG; jeo:JMA_23050; -.
DR HOGENOM; CLU_014322_1_0_9; -.
DR OrthoDB; 9806267at2; -.
DR BioCyc; JESP1508404:G14D9-11560-MONOMER; -.
DR Proteomes; UP000031449; Chromosome.
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; 2.30.30.40; SH3 Domains; 4.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR017293; N-acetylmuramoyl-L-ala_amidase.
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; 4.
DR PIRSF; PIRSF037846; Autolysin_YrvJ_prd; 2.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 4.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 4.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AJD91622.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..512
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002113376"
FT DOMAIN 25..87
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 100..162
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 173..235
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 248..310
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 512 AA; 55265 MW; BB82DB00FBF6F00A CRC64;
MKLLSVLLST VLLLSLFPHL EANAEENAVE SAYDGILIRE GPGLSYPAIA SGQAGEQFNE
LQRANGWVEV ALDEGSGWIA EWLLVSSSEP PSEPSTVSEE SNATILVDRL NVRDDFSLDG
LVIGTLNTGD QVNVSDEKYG WLYISSDNIS GWVSSDYVEY NSSSAVQTSE PATDDIHITV
NTLNVRAEPD RNADVVGSVN LYDSFTVKEQ SGGWLKIDFG DNTGWIASWF TERGFHPGGS
TQQAAGLDET VTILYNGSNI RQEPSTDAAV IYKASSGEAM EIVGLSGDWY EIALPGGATG
YIANWIVSTE GNSETAQEVE ATEQPEEPKE PVTSIADATI VIDAGHGGRD GGAVGAAGTL
EKSLTIRTAE VLYHMLSGTG ANVIMTREDD RYVDLYSRVT TSRDHQADVF ISLHYDAIND
RSVKGFTTYY YGGPDEDLAD AVHAGLSDSM TVKNRGIKHG NFLVLRDNSA PSVLLELGFI
SNPSEEATIN NDRFREMAAT GIYNGLTEYF SQ
//
