ID A0A0R2H2Y4_9LACO Unreviewed; 765 AA.
AC A0A0R2H2Y4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase domain-containing protein {ECO:0000259|SMART:SM00644};
GN ORFNames=IV41_GL001239 {ECO:0000313|EMBL:KRN43828.1};
OS Limosilactobacillus ingluviei.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=148604 {ECO:0000313|EMBL:KRN43828.1, ECO:0000313|Proteomes:UP000051639};
RN [1] {ECO:0000313|EMBL:KRN43828.1, ECO:0000313|Proteomes:UP000051639}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14792 {ECO:0000313|EMBL:KRN43828.1,
RC ECO:0000313|Proteomes:UP000051639};
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 -!- 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:KRN43828.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JQBA01000032; KRN43828.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2H2Y4; -.
DR PATRIC; fig|148604.4.peg.1275; -.
DR Proteomes; UP000051639; 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; cd06583; PGRP; 1.
DR Gene3D; 2.10.270.10; Cholin Binding; 6.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF01473; Choline_bind_1; 3.
DR Pfam; PF19127; Choline_bind_3; 2.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 3.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS51170; CW; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000051639};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 328..347
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 604..744
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 765 AA; 85663 MW; ECAC4D3A987D70AE CRC64;
MLASAATPTS STTDATTMSQ TIQAVAPQSP TENAQSVAAQ PVANNEQTAS EVKIASSTPT
QDVPKVNGTE SYEQGHWYLK NSAGQPLNGW QNLSDNRLAY YSPETNWMQY GEQNIDGKWY
FFDQFNGDVK TGWYQLPDGR RVYYDVQKGD HAVSGQGMLH GMQPVADGTY YYFNPGYGTQ
ESGLKQVNGQ TYYFAPAQVR SAEANLDGHW YYFKADGAMA TGFTQLKDGR TVYYNPKGWM
QYGEQNINGK WYFFDKVDGH MAKKWFTLPD GRLVYYQVDA NGAGQGMLHG LSEINGQKYY
FDPGMGTRRT GLQVVNGKTY YFNPAMVQTA EVNFGGHWYY FKADGTMATG FIQLKDGRTV
YYNPKGWMQY GEQNIDGKWY FFNQRDGHMA IGWQALPDGR KVYYDVDAKG QGRGMIHGYN
LIDGVLYNFD PVYGTLIGKV TNDLFYDATT GQLQYYNADG KLVKDQAVKL GNQTYQADAQ
GNLQITGDGE HAINGHWYLY DAKNGKFKTS WQTLADGRTV YYGPQAYMLY GHQTIDGHGY
FFNRVNGDLT KGWLQDGHDW YYYNPNNGQA QTGTATINGV TYRFDNSGKQ ILNYAIDYRY
ALNAGEGDED TAANNYIVLH EVGTESGGAA NANYFKQDWE KVEAYTTFVV GDGGRVYQVG
RPGQVSWGAG RVANHNAPVQ IELGRTYNAS QFWQDYTAYV RLARDMAGKF GIPLTLDAGG
AGTRGIKSHN WVSHNIWGDH VDPYGYLARF GVTQAKLAHD LQYGI
//
