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Database: UniProt
Entry: A0A2R3JU85_9LACO
LinkDB: A0A2R3JU85_9LACO
Original site: A0A2R3JU85_9LACO 
ID   A0A2R3JU85_9LACO        Unreviewed;       282 AA.
AC   A0A2R3JU85;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:AVK63120.1};
GN   ORFNames=C5Z26_02820 {ECO:0000313|EMBL:AVK63120.1};
OS   Lactobacillus sp. CBA3606.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=2099789 {ECO:0000313|EMBL:AVK63120.1, ECO:0000313|Proteomes:UP000238064};
RN   [1] {ECO:0000313|EMBL:AVK63120.1, ECO:0000313|Proteomes:UP000238064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBA3606 {ECO:0000313|EMBL:AVK63120.1,
RC   ECO:0000313|Proteomes:UP000238064};
RA   Jung M.Y.;
RT   "Complete genome sequence of Lactobacillus sp. CBA3606.";
RL   Submitted (FEB-2018) 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; CP027194; AVK63120.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R3JU85; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000238064; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 1.
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; 1.
DR   PIRSF; PIRSF037846; Autolysin_YrvJ_prd; 2.
DR   SMART; SM00646; Ami_3; 1.
DR   SMART; SM00287; SH3b; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51781; SH3B; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..93
FT                   /note="SH3b"
FT                   /evidence="ECO:0000259|PROSITE:PS51781"
SQ   SEQUENCE   282 AA;  31218 MW;  E3E743889E360511 CRC64;
     MQVLKRFWRQ ITVTLIFIGL VAGFTFLLAT HNTAVVNIAN VNIRQGPGMS YAITDATTKG
     TKVHIVRRKN NWLYVRYADH KFGWIASWLV NENNSQLTRT TKISEATIVI DPGHGGSDSG
     ALSSKGKMEK TYTLRVAKVV AKRLRAAGAH VVLTRDTDKW VSLTNRPAVA NKLHADAFIS
     FHFDSTAEKN QASGITTYYY HKSTSLGLAN ALSSDVDALP IRNKGTEFGD FLVIRDNQVP
     AVLMELGYIN DKSDFKTISS KKYPNEVAHA VYAGLSTYFA NQ
//
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