ID A0A3E2JN18_9BACI Unreviewed; 467 AA.
AC A0A3E2JN18;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=SH3b domain-containing protein {ECO:0000259|PROSITE:PS51781};
GN ORFNames=D0463_08220 {ECO:0000313|EMBL:RFU67042.1};
OS Bacillus sp. V59.32b.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1758642 {ECO:0000313|EMBL:RFU67042.1, ECO:0000313|Proteomes:UP000258625};
RN [1] {ECO:0000313|EMBL:RFU67042.1, ECO:0000313|Proteomes:UP000258625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=V59.32a {ECO:0000313|EMBL:RFU67042.1,
RC ECO:0000313|Proteomes:UP000258625};
RA Seuylemezian A., Vaishampayan P.;
RT "Bacillus chawlae sp. nov., Bacillus glennii sp. nov., and Bacillus saganii
RT sp. nov. Isolated from the Vehicle Assembly Building at Kennedy Space
RT Center where the Viking Spacecraft were Assembled.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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:RFU67042.1}.
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DR EMBL; QVTC01000030; RFU67042.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2JN18; -.
DR Proteomes; UP000258625; Unassembled WGS sequence.
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; 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 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:UP000258625};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 68..131
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 142..205
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT DOMAIN 221..285
FT /note="SH3b"
FT /evidence="ECO:0000259|PROSITE:PS51781"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 50201 MW; 63C076CCE6E7489F CRC64;
MQLLSTFGRS RPHRPRLSGT TKKGRRLPSP NNKMDGPRFL SVKKTGWVSS KYVTVIKPTA
SKAAVASGTK YYVTATTLNI RKSPSTSAAR VDSVKKNAAV TLYEKKGSWG RVKTASGKTG
WASLSYLTTK APAAPKPAAK APAKYYVTAT SLNIRKSPST TAAKVDLVKK NAAVSLYEKK
GSWGKVKTAS GKTGWASLSY LTTKAPVAPK PAPKPPVTTS SGKSYVVIRT DGVNIRKSAS
TSAAVVTKVN RGTKLEKISV DNGWVQVKTS TGKTGWVANW LATTAGKGVR GKVIVLDPGH
GGTDSGAVGK THNERSINLS TANELKTLLQ NAGAKVIMTR TSNTSRKLEL SERVAISHQY
KPDVFISIHY NSGGNATGID TFYDAKYGNE KELATSIQNE LIKSTGKKNR GVKPAEFYVV
KYNEMPSILV ELGFISNPTE EKEIATKAYQ QKAARGIYNG LNKYFNL
//
