ID A0A0M4G341_9BACI Unreviewed; 403 AA.
AC A0A0M4G341;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=SH3b domain-containing protein {ECO:0000259|PROSITE:PS51781};
GN ORFNames=AM500_02305 {ECO:0000313|EMBL:ALC88760.1};
OS Bacillus sp. FJAT-18017.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC88760.1, ECO:0000313|Proteomes:UP000060713};
RN [1] {ECO:0000313|EMBL:ALC88760.1, ECO:0000313|Proteomes:UP000060713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC88760.1,
RC ECO:0000313|Proteomes:UP000060713};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) 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; CP012602; ALC88760.1; -; Genomic_DNA.
DR RefSeq; WP_053597753.1; NZ_CP012602.1.
DR AlphaFoldDB; A0A0M4G341; -.
DR STRING; 1705566.AM500_02305; -.
DR PATRIC; fig|1705566.3.peg.469; -.
DR Proteomes; UP000060713; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 3.
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; 3.
DR PIRSF; PIRSF037846; Autolysin_YrvJ_prd; 3.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 3.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 3.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000060713};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..403
FT /note="SH3b domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005794617"
FT DOMAIN 33..94
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 95..159
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 160..223
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
SQ SEQUENCE 403 AA; 43505 MW; 0BE12DAE6C362420 CRC64;
MKVASLVKSV VCLLVLFSFV LSLDHNKAEA AYSFQAKVTA SSLNVRSGPG TTYAVIGKLT
TGKIVTVLQQ KNGWSSITAG TVKGWVSSQY LSPVTWTGYV TADSLNVRKA ASATATILGA
IPRGTAVTVH GTDGGWLKVT VPSKSLSGWV SSSYISKTAA YPKLVLKSAT TMRKGPGTSY
AIISSESPGT YYDKLAVKNG WTQVKKSNGT TGWIVSTLLR DPATVLKGKV IVLDAGHGGY
DSGAVGAIYY EKMLTLKTVL QLGPKLQKSG AKVVYTRTTD TYLTLAKRVS ISNLNLAHAF
LSIHYNAFSK TSTGIETYYY YYSRERSLAS SIQNGIIKQT GMRNLGAKYG NYHVLRENKR
PSALLELGFI SNPYEEKTIA SSTFQTKAVQ GIHDGLFNYF LNR
//
