ID A0A1Y0RUA7_9CYAN Unreviewed; 664 AA.
AC A0A1Y0RUA7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:ARV62318.1};
GN ORFNames=BZZ01_30130 {ECO:0000313|EMBL:ARV62318.1};
OS Nostocales cyanobacterium HT-58-2.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales.
OX NCBI_TaxID=1940762 {ECO:0000313|EMBL:ARV62318.1, ECO:0000313|Proteomes:UP000196302};
RN [1] {ECO:0000313|EMBL:ARV62318.1, ECO:0000313|Proteomes:UP000196302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HT-58-2 {ECO:0000313|EMBL:ARV62318.1,
RC ECO:0000313|Proteomes:UP000196302};
RA Hughes R.-A., Zhang Y., Zhang R., Williams P.G., Lindsey J.S., Miller E.S.;
RT "Genome sequences and microbial community composition of HT-58-2, a
RT tolyporphin-producing cyanobacterium-microbial holobiont.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP019636; ARV62318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y0RUA7; -.
DR KEGG; ncn:BZZ01_30130; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000196302; Chromosome.
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; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
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; PF11741; AMIN; 2.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000196302};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..664
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012259800"
FT DOMAIN 549..658
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 301..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..470
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 72125 MW; 917F941664E61E57 CRC64;
MKINWLLPGT FAMTAIFMLL SPAQAAKLQS WRFDASQNQL EINTEGPVQP QAQLVFNPTR
LVIDLPGTDS GRPQLIQPVK SSAIRAVRVG QFDGQTTRIV VELTPGYTLD PKQVKFEGKT
ASRWIVQLPT PQVEQVASSS PNTSFNVYSV VRSGSNSTAH QSTSINNNSV DNNDTVVNTL
EGSTQKETVT SNAQGLTQIE SLRVTGDGLF VRTNGRSPRI QIFRSSDKSA VNIDILDAAL
SPRLSQQVVP INKYGVKRVE FTQLKTTPGV RMTLWVDKNS PDWQASTSSF GGLVILPSGD
RNKLSRDARD NSSSLVNSDM TTGSVNSRNP NLTSPTSDSL STIQSVELTA SGNQLLIKGD
QPLSANGGWD RVSSMFRITI PNAKLAAAVR GPNFDASSPI LRVRLQQQDP RTVVVYIQPA
AGVQIGQLNQ LSGQLLSLEL QRSFSPLTPR VSLPPLPRPN PRPLPPITSN PLPMPQPQLR
PPVPNGRVVV VVDPGHGGKD SGAPGLGGLL EKDVVLPIGS RIATILQQNG VQVVLTRDAD
YFVELQGRVD IADRSNADLF VSVHSNSVDG RPDVNGLETY YYDSGLGLAR VVHSTILQSI
PTLKDRGVRK ARFYVLRKSS MPSILVETGY MTGQEDNPRL GSPEYQNRMA EAIANGILLY
LRQR
//