ID A0A1D9FQW7_9CLOT Unreviewed; 749 AA.
AC A0A1D9FQW7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN ORFNames=BJL90_18860 {ECO:0000313|EMBL:AOY77736.1};
OS Clostridium formicaceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1497 {ECO:0000313|EMBL:AOY77736.1, ECO:0000313|Proteomes:UP000177894};
RN [1] {ECO:0000313|EMBL:AOY77736.1, ECO:0000313|Proteomes:UP000177894}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27076 {ECO:0000313|EMBL:AOY77736.1,
RC ECO:0000313|Proteomes:UP000177894};
RA Bao T., Cheng C., Zhao J., Yang S.-T., Wang J., Wang M.;
RT "Complete Genome Sequence of Acetogen Clostridium formicoaceticum ATCC
RT 27076.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP017603; AOY77736.1; -; Genomic_DNA.
DR RefSeq; WP_070971781.1; NZ_CP020559.1.
DR AlphaFoldDB; A0A1D9FQW7; -.
DR STRING; 1497.BJL90_18860; -.
DR KEGG; cfm:BJL90_18860; -.
DR OrthoDB; 9809488at2; -.
DR Proteomes; UP000177894; 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; cd12797; M23_peptidase; 1.
DR CDD; cd07341; M56_BlaR1_MecR1_like; 1.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR016047; Peptidase_M23.
DR InterPro; IPR008756; Peptidase_M56.
DR PANTHER; PTHR21666:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR Pfam; PF05569; Peptidase_M56; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..368
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 481..597
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 749 AA; 85573 MW; 866B2CCD081F0B28 CRC64;
MDILGGIFLH VLYLSLTTSI LMIAYLLIKK LFLQRIAMRY HHIIWMVLII RLLMPINIES
SISIFNFFPQ KSLVILETYV EKNSSNTFTT GETVPVYRTL DFKKNGGTKH EFYIEENHMF
DDFSAYDPAE LNENTIGKEP NEWIIKVFSR IWLLGMLLLT LFFYSTLLVF ERKYKMLKKP
IIPELEFLAE KCRKKMNIRK TIPIYLNDCL KTPCIRGVIN PCIYLPTDIY AKTDYSELQY
IILHEMAHYK RKDLIYNLAT LMVALIHWFN PLLWIVIKHI RHDREIACDA YVMETIEEEE
IIPYGMTLIN LAKRFTSKDS KFYLVSFCEG NSLLERRIKM IKMFKKGSYR ISIAAIIFLI
IIGGVILTNP SRFESINLIS TSQTVEDSAA KELEKENLLD NTKEEEPNYK DIIKDMLVLI
DPGHGGDDPG AIYTGGNLVE IKEKDVSLEI SLLLYNMLKE SGINAELTRR EDISISLENR
MELVNQLNPS LFVSIHNNFG GVSERDVLTL SYTSISKDLR RTTGERAAQI IHKELVNVIE
NKDSEILEMS NRLKFSSIKI PAVIIEPAYI GNHSSTENLL TEEFKKQIAL SIHDGIIKVL
KEMAADIQES NNQSEEIILN TKGQWPVPEY SRISSRYGEA IHPISKDKRF HTGIDISAPE
GKTIVAFKDG KVVRAGELRD HGKTIVIDHG SGLVTLYAHA SKLNASVGDE VKEGQKIAEI
GSTGGATGNH VHFEIWINGK HVNPIDYLR
//
