ID S3AER8_9STRE Unreviewed; 561 AA.
AC S3AER8;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN ORFNames=HMPREF1481_00752 {ECO:0000313|EMBL:EPD87663.1};
OS Streptococcus sp. HPH0090.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1203590 {ECO:0000313|EMBL:EPD87663.1, ECO:0000313|Proteomes:UP000014396};
RN [1] {ECO:0000313|EMBL:EPD87663.1, ECO:0000313|Proteomes:UP000014396}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HPH0090 {ECO:0000313|EMBL:EPD87663.1,
RC ECO:0000313|Proteomes:UP000014396};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dover J., Dai D.,
RA Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptococcus sp. HPH0090.";
RL Submitted (APR-2013) 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:EPD87663.1}.
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DR EMBL; ATCD01000001; EPD87663.1; -; Genomic_DNA.
DR RefSeq; WP_016466085.1; NZ_KE150464.1.
DR AlphaFoldDB; S3AER8; -.
DR STRING; 1203590.HMPREF1481_00752; -.
DR PATRIC; fig|1203590.3.peg.723; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG5263; Bacteria.
DR HOGENOM; CLU_035498_0_0_9; -.
DR Proteomes; UP000014396; 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; 2.10.270.10; Cholin Binding; 3.
DR Gene3D; 2.20.120.10; Multimodular pneumococcal cell wall endolysin, domain 3; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR018337; Cell_wall/Cho-bd_repeat.
DR InterPro; IPR002508; MurNAc-LAA_cat.
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; PF01473; Choline_bind_1; 3.
DR Pfam; PF19085; Choline_bind_2; 1.
DR Pfam; PF19127; Choline_bind_3; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF69360; Cell wall binding repeat; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51170; CW; 3.
PE 4: Predicted;
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..561
FT /note="MurNAc-LAA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004505479"
FT REPEAT 110..129
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 169..188
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT REPEAT 228..247
FT /note="Cell wall-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00591"
FT DOMAIN 425..555
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 24..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 561 AA; 63514 MW; 84CA019EDBBF5E67 CRC64;
MKKTFLASAI TLTYLGLATN PALAEENKVQ TTTVETTQET TTANKVETKE PSTKETVPST
EASSSLPTTS TTAPNTSPAK KEESKAPEVI KEGWVFEGNI WRFYEANKAA INWKKIHGKW
YYFDKDGIML SDTIYDGYIL TSNGAMVDSG WGKIKDKWYY ANPSGRIVKK DWKKVGGVWY
YFDKEGIMLS NTIFDGYIFT NSGAMAESAW VKQDGKWYYA QASGSLIKNK WDKIGGVWYY
FNKDAIMASN QWQGSYYLKA SGAMAEREWI FDKNYNSWFY LKSGGTYAAR EWIGSYYLKA
GGYMAKNEWI FDNYYNAWYY LEESGIYVTG TRKIDGKAHQ FQSNGKWIGE VPISRGFEKG
KYTKTVFLDP GHGGKDPGAV YYNTNEKDLT LQVYKKLRKE LQGLGYTVLS SRDSDVYVDF
VTERSKMVNK TNSDIFISIH FNASGAPASN RSGIQTYSYE EDPGYSSKIN QYWHNHPDRI
SESNRLAADI HSSLLAETGA KDAGLLQSSF AVLRETDKPA VLLELGYIDN FNENQQIRSD
AYQNRLVAGI VKGIQKYYAG K
//
