ID A0A0A6Y1F3_9FLAO Unreviewed; 369 AA.
AC A0A0A6Y1F3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:KHE69079.1};
GN ORFNames=HMPREF9074_08681 {ECO:0000313|EMBL:KHE69079.1};
OS Capnocytophaga sp. oral taxon 329 str. F0087.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE69079.1, ECO:0000313|Proteomes:UP000030579};
RN [1] {ECO:0000313|EMBL:KHE69079.1, ECO:0000313|Proteomes:UP000030579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0087 {ECO:0000313|EMBL:KHE69079.1,
RC ECO:0000313|Proteomes:UP000030579};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (OCT-2014) 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:KHE69079.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFHP02000131; KHE69079.1; -; Genomic_DNA.
DR RefSeq; WP_009391219.1; NZ_KN390015.1.
DR AlphaFoldDB; A0A0A6Y1F3; -.
DR STRING; 706436.HMPREF9074_08681; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_4_5_10; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000030579; 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; 3.40.630.40; Zn-dependent exopeptidases; 1.
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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
FT DOMAIN 89..246
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 263..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 41536 MW; FDA449CC65C66A16 CRC64;
MKLLRLILFW LCWAIPLSGY AQKTPVFKVV LDAGHGGKDP GKVVNKTIYE KDVVLKIALL
VGKKLEAHPD IKVIYTRKTD ELIDLYERGA IANKNKADVF VSIHCNAHET QVEGAETYVL
GLNANEQNFE VAKAENSVIY LEDDYKKKYA QYNINSPESI IGLSIMQEEF LEQSIQLAKI
VQSQLTGVMK RANRGVRQAG FIVLHQTYMP SILIETAFLT NNEERKFLTS EKGQEEFAEN
IATAILTYKK WIQGQSSYVA PSDTVSVHGT GRKQPANHPT EKGSVSYKVQ ISSSPKRLEA
KPFNFKGLSP ISTEKDGKVY VYYYGNAKRH KEALTLLSNA KKKGYKDAYI AAFYLGKRIT
IEKAKQIEK
//