ID A0A0D5NMP1_9BACL Unreviewed; 367 AA.
AC A0A0D5NMP1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=SH3b domain-containing protein {ECO:0000259|PROSITE:PS51781};
GN ORFNames=VN24_18390 {ECO:0000313|EMBL:AJY76168.1};
OS Paenibacillus beijingensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1126833 {ECO:0000313|EMBL:AJY76168.1, ECO:0000313|Proteomes:UP000032633};
RN [1] {ECO:0000313|EMBL:AJY76168.1, ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|EMBL:AJY76168.1,
RC ECO:0000313|Proteomes:UP000032633};
RX PubMed=25937453; DOI=10.1016/j.jbiotec.2015.04.015;
RA Kwak Y., Shin J.H.;
RT "Complete genome sequence of Paenibacillus beijingensis 7188(T) (=DSM
RT 24997(T)), a novel rhizobacterium from jujube garden soil.";
RL J. Biotechnol. 206:75-76(2015).
RN [2] {ECO:0000313|Proteomes:UP000032633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24997 {ECO:0000313|Proteomes:UP000032633};
RA Kwak Y., Shin J.-H.;
RT "Genome sequence of Paenibacillus beijingensis strain DSM 24997T.";
RL Submitted (MAR-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; CP011058; AJY76168.1; -; Genomic_DNA.
DR RefSeq; WP_045671596.1; NZ_CP011058.1.
DR AlphaFoldDB; A0A0D5NMP1; -.
DR STRING; 1126833.VN24_18390; -.
DR KEGG; pbj:VN24_18390; -.
DR PATRIC; fig|1126833.4.peg.4048; -.
DR HOGENOM; CLU_014322_1_0_9; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000032633; 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; 2.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR003646; SH3-like_bac-type.
DR InterPro; IPR036028; SH3-like_dom_sf.
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; 2.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00287; SH3b; 2.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51781; SH3B; 2.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032633};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..367
FT /note="SH3b domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002296550"
FT DOMAIN 27..89
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 105..171
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT REGION 96..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 367 AA; 39141 MW; 82A64AD3484801B9 CRC64;
MRRSLFGALV FALLLTGPQT GEAAGSSGVY RVAADSLNVR EEPDGKARVV GVLKARTIVR
VSDDQYGWVK VKAGETTGWA AGHYLKKADG AAVADASSGK STSRAKSARS AASLGDSVRL
RKGPGTGYEV IGSVNKGDRL TVLESEDGWK RVRTADGTVG WMSGQYVGSA ANIEAVSAVK
NVSSRTGSIR GKVIVIDPGH GGSDPGMIGT KHETLEKDLT LSTSVLVADR LRTLGAQVIM
TRTKDSQKPA LSERVRISEM AGADAFVSIH FNSSEQDTSG SLTFYYSKQK DERLARAIEG
RLSQRIGLKS NGISFGDFHV LRENDTPSAL VELGFLSNAS DEEIVRTKSY QRKAAAAIVE
GFKDYFE
//
