ID A0A1Q3RJZ4_9FIRM Unreviewed; 965 AA.
AC A0A1Q3RJZ4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN ORFNames=BGO41_12660 {ECO:0000313|EMBL:OJV64462.1};
OS Clostridiales bacterium 38-18.
OC Bacteria; Bacillota; Clostridia; Eubacteriales.
OX NCBI_TaxID=1895746 {ECO:0000313|EMBL:OJV64462.1, ECO:0000313|Proteomes:UP000185881};
RN [1] {ECO:0000313|EMBL:OJV64462.1, ECO:0000313|Proteomes:UP000185881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=38-18 {ECO:0000313|EMBL:OJV64462.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:OJV64462.1}.
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DR EMBL; MKTL01000006; OJV64462.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3RJZ4; -.
DR STRING; 1895746.BGO41_12660; -.
DR Proteomes; UP000185881; 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; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR003790; GHL10.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR43405; GLYCOSYL HYDROLASE DIGH; 1.
DR PANTHER; PTHR43405:SF1; GLYCOSYL HYDROLASE DIGH; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF02638; GHL10; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..965
FT /note="MurNAc-LAA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013179674"
FT DOMAIN 849..959
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 965 AA; 106745 MW; B4C2AD33EAE0A774 CRC64;
MKTKISLLLT VILLMTLSLS FADGLSDAQK NEINGSFKGL WVATVLNLDY PVKATTNVDT
LKKEAIEILD KAQSMGLNAI VLQVRPAGDA IYSSAYFPWS KYLTGKQGTA PADGFDPLAF
WIDEAHKRNL ELHAWINPYR ITRKNASDPS YDYSSLAANH PARLHPDWVV EHTDGNLYFD
PGNPEVRKYL VDSINELITK YDVDGIHFDD YFYPGTTFND DKTYAKYGSK FNSKADWRRN
NVDQLIKEVK SLIDTKKPIV QFGISPFGIW ANAKNKSGGS DTSGFESYFN QYADTKKWVE
EEWIDYIAPQ LYWEIGYSVA DYSKLVKWWS NVVDGTDVHL YIGQAAYRTG DKSSSSPWYG
VDEIARQLQL NESYDEVSGS IFFRYAFFKA SPTLSALLTD YYNGTLANAT INTKLTIGRP
VKDVSTTSSY YFVGGASNPN SPLYINGEEV IIRTKDGYFG KYVALKSGKN TFVVSQDGKT
ATRVITKVGA TLATPMTKAE IIAGSTWPQS ATMINETEEF KFYCRAPIGA KVTATLGGKT
YTLTPETTKN ASNKLYSTAY SLKIKAPVQT GSARIVDYGK PVYTMSYNGV TNTQSGNVNV
RVIMKNAPFI ATVSSTNVDS YQSASASNGA HYILQTGMTD LVTGINGDYI RLSSGIWVKS
KSVELKDQKM PSIQIKSIAN TVAARTETLK FELSSLPIAS AEFDGEKLKI TINKASNSVQ
IPLKSNSMIK SAVSKSDQDK ITYELTFKDA KTFAGHNLEV LGNQIIITLK TKFVASGELP
LKGAIILLDA GHGGSDTGAI GLLGYEYPEK MVNFNIVKQL ENELKLKGAT VVLTRTSDDY
VSLDTRLSQS MKLSPDMLIS IHADSLEDTA DLTKTSGFTV YYKESLSKSL ANNLSKAIDT
EFDLYNRGVK NMNFYIVRNT WTPSVLIETG FMPSPSDFQI LSNSIDQKRY AKTLTNAIVN
YFSGE
//
