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Database: UniProt
Entry: A0A0R2HZ24_9LACO
LinkDB: A0A0R2HZ24_9LACO
Original site: A0A0R2HZ24_9LACO 
ID   A0A0R2HZ24_9LACO        Unreviewed;       290 AA.
AC   A0A0R2HZ24;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN   ORFNames=IV83_GL001935 {ECO:0000313|EMBL:KRN58073.1};
OS   Pediococcus inopinatus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=114090 {ECO:0000313|EMBL:KRN58073.1, ECO:0000313|Proteomes:UP000051698};
RN   [1] {ECO:0000313|EMBL:KRN58073.1, ECO:0000313|Proteomes:UP000051698}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20285 {ECO:0000313|EMBL:KRN58073.1,
RC   ECO:0000313|Proteomes:UP000051698};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRN58073.1}.
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DR   EMBL; JQBC01000078; KRN58073.1; -; Genomic_DNA.
DR   RefSeq; WP_046870601.1; NZ_JQBC01000078.1.
DR   AlphaFoldDB; A0A0R2HZ24; -.
DR   PATRIC; fig|114090.3.peg.2015; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000051698; Unassembled WGS sequence.
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; 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   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 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        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          178..286
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   290 AA;  33034 MW;  6916E3129BDF9EAD CRC64;
     MIKDLSTLIN NKIPFWKQPL FILRVIIIVG LVYIVGHLTI QYFCEPKVTA QTINLRDMPT
     PKGHIIEKLA YGTRLKVEKK NVHTKWWRVK VGHHQGWVAS WLIHQTKYRA INSLAEATIV
     LDPGHGGIDS GTIGLHGAME KTYTLPTALA VAQLLRSKYS RVILTRQSDQ SVSLSKRPKI
     ANMDKATLFI SFHFNSAGKK NAAQGFEVFQ YHQNARKLAQ KLNNNFVNLP LVNRGIAFGD
     FEVLRDNQRP AVLIEMGFMD STHDFKHIKS KIYQRLVARD VVRGITQYVH
//
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