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Database: UniProt
Entry: A0A3B0BXT3_9BACL
LinkDB: A0A3B0BXT3_9BACL
Original site: A0A3B0BXT3_9BACL 
ID   A0A3B0BXT3_9BACL        Unreviewed;       374 AA.
AC   A0A3B0BXT3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 12.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:RKN77134.1};
GN   ORFNames=D7M11_24240 {ECO:0000313|EMBL:RKN77134.1};
OS   Paenibacillus ginsengarvi.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=400777 {ECO:0000313|EMBL:RKN77134.1, ECO:0000313|Proteomes:UP000282311};
RN   [1] {ECO:0000313|EMBL:RKN77134.1, ECO:0000313|Proteomes:UP000282311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 13059 {ECO:0000313|EMBL:RKN77134.1,
RC   ECO:0000313|Proteomes:UP000282311};
RX   PubMed=17684262; DOI=10.1099/ijs.0.64906-0;
RA   Yoon M.H., Ten L.N., Im W.T.;
RT   "Paenibacillus ginsengarvi sp. nov., isolated from soil from ginseng
RT   cultivation.";
RL   Int. J. Syst. Evol. Microbiol. 57:1810-1814(2007).
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:RKN77134.1}.
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DR   EMBL; RBAH01000020; RKN77134.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0BXT3; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000282311; 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; 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:UP000282311};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..374
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017224295"
FT   DOMAIN          29..92
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
FT   DOMAIN          117..180
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
SQ   SEQUENCE   374 AA;  39641 MW;  123F93C0A227F6DC CRC64;
     MKSFARNALA LGGVLLGIWL FPANEASAET YAAKVDADVL NVRAEPASRA SVIGSLTKGT
     AVTVSDEAYG WAQVKLGSKT GWVAAQYLVK TGTVKQQTAV KSETVVKTAA VTSASAAKEG
     VVTADMLWMR EGSGTDSKEK ELLVKGTRLA ITGGKDGWLQ VKTPGGAVGW VSERYVGQPG
     SVEVQSQKPA QGGLRDKVIV IDPGHGGGDP GVIGLTHKTE EKKINLSTAE LVADELRRAG
     AKVIMTRKSD GEQPELSERA AVSNKQQADA FVSIHYNASP KKVSGTLVYY YSESKDRTLA
     RAIEGRLAKG NGLLKSNGIS FGDYHVLREN KQPAVLLELG FLTDSRDEAT VRKDDYQRKA
     AAAIAAGLAD YFGD
//
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