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Database: UniProt
Entry: A0A089L4E4_9BACL
LinkDB: A0A089L4E4_9BACL
Original site: A0A089L4E4_9BACL 
ID   A0A089L4E4_9BACL        Unreviewed;       375 AA.
AC   A0A089L4E4;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=SH3b domain-containing protein {ECO:0000259|PROSITE:PS51781};
GN   ORFNames=R70331_27880 {ECO:0000313|EMBL:AIQ54935.1};
OS   Paenibacillus sp. FSL R7-0331.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1536773 {ECO:0000313|EMBL:AIQ54935.1, ECO:0000313|Proteomes:UP000029487};
RN   [1] {ECO:0000313|EMBL:AIQ54935.1, ECO:0000313|Proteomes:UP000029487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FSL R7-0331 {ECO:0000313|EMBL:AIQ54935.1,
RC   ECO:0000313|Proteomes:UP000029487};
RA   den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT   "Comparative genomics of the Paenibacillus odorifer group.";
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; CP009284; AIQ54935.1; -; Genomic_DNA.
DR   RefSeq; WP_042180941.1; NZ_CP009284.1.
DR   AlphaFoldDB; A0A089L4E4; -.
DR   STRING; 1536773.R70331_27880; -.
DR   KEGG; paee:R70331_27880; -.
DR   eggNOG; COG0860; Bacteria.
DR   eggNOG; COG3103; Bacteria.
DR   HOGENOM; CLU_014322_1_0_9; -.
DR   Proteomes; UP000029487; 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   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; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51781; SH3B; 2.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000029487};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..375
FT                   /note="SH3b domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001846021"
FT   DOMAIN          30..92
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          113..176
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
SQ   SEQUENCE   375 AA;  39016 MW;  F56496A190383E13 CRC64;
     MIKSIHKALL LAGLLTGALL TFCQAEAAAA YTAKVYASSL TVRSEPAAGA SAVGFIKNGT
     TVTVTDEQHG WMKVRSGSVT GWVAGYYLKK VDGGSASTAA GSSVSTVKAS SGSSSATVTA
     DSLRIRGGPG TGYAVVGSLK AKDKVTVLAR QDGWARIKTT AGEIGWVSAQ YLSGGGSSSG
     VTTASATSTS SKGVSKIGSK LIVIDAGHGG SDPGMLGTTY NTMEKDLTLQ TAFYLRDYLT
     AKGATVQMTR TTASQKPTLA RRVQIGHSAD ADAFVSIHYN SSPKNVSGTL TFFYSESDDL
     RLARAIENRL GQGIGLKSNG LSYGNYHILR ENRVPAALVE LGFLSNPYDE AIVRTSSYQK
     KAAKAIAEGL ADYFK
//
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