ID H3K869_9FIRM Unreviewed; 366 AA.
AC H3K869;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase CwlD {ECO:0000313|EMBL:EHR36467.1};
GN ORFNames=HMPREF9454_01442 {ECO:0000313|EMBL:EHR36467.1};
OS Megamonas funiformis YIT 11815.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Megamonas.
OX NCBI_TaxID=742816 {ECO:0000313|EMBL:EHR36467.1, ECO:0000313|Proteomes:UP000005963};
RN [1] {ECO:0000313|EMBL:EHR36467.1, ECO:0000313|Proteomes:UP000005963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 11815 {ECO:0000313|EMBL:EHR36467.1,
RC ECO:0000313|Proteomes:UP000005963};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Morotomi M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Megamonas funiformis YIT 11815.";
RL Submitted (JAN-2012) 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:EHR36467.1}.
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DR EMBL; ADMB01000066; EHR36467.1; -; Genomic_DNA.
DR RefSeq; WP_008538770.1; NZ_JH601090.1.
DR AlphaFoldDB; H3K869; -.
DR STRING; 437897.GCA_900128435_01767; -.
DR GeneID; 69726208; -.
DR PATRIC; fig|742816.3.peg.1390; -.
DR HOGENOM; CLU_014322_2_0_9; -.
DR OrthoDB; 9772024at2; -.
DR Proteomes; UP000005963; 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; 2.60.40.3500; -; 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; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..366
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003587780"
FT DOMAIN 249..360
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 180..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 366 AA; 39956 MW; 9824A9882D518BB0 CRC64;
MRKSLYIFSL VCLFTLLCMQ SMVFAASETA TIKNLRISNN SDKVRIVVDA DKEVDYQSFA
LSSPDRVVID LNDAALAKNI EKEVDINSKY ASKVRVAQFK DNVVRVVVET DVKKSGYDIF
GIVGGETPYR VAMDFGNISY AAIGSTTGSS TSSSSNDTSY RVNEDFDIDK NAKSVLKGKR
ITIDPGHGGS DSGAIGPTGV REKDPTLRIG LNLAEMLKQS GAKVYITRKT DTDVAPQPAT
DVEELQARVD VGNKTNSDIF VSIHLDSFTS PSAQGTTGYY YVNGSSNSER LARYIKEGVI
EQIGTYDRGT KTSNFYVVKH TQMPATLLEV AFVSNPKEEA ILKSDDGVKK SAKGIFNGIV
RYFSEL
//