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Database: UniProt
Entry: A0A1I4C0G0_9FIRM
LinkDB: A0A1I4C0G0_9FIRM
Original site: A0A1I4C0G0_9FIRM 
ID   A0A1I4C0G0_9FIRM        Unreviewed;      1068 AA.
AC   A0A1I4C0G0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000313|EMBL:SFK74564.1};
GN   ORFNames=SAMN05216390_10386 {ECO:0000313|EMBL:SFK74564.1};
OS   Lachnospiraceae bacterium KH1T2.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1855374 {ECO:0000313|EMBL:SFK74564.1, ECO:0000313|Proteomes:UP000198626};
RN   [1] {ECO:0000313|EMBL:SFK74564.1, ECO:0000313|Proteomes:UP000198626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH1T2 {ECO:0000313|EMBL:SFK74564.1,
RC   ECO:0000313|Proteomes:UP000198626};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOSY01000003; SFK74564.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4C0G0; -.
DR   STRING; 1855374.SAMN05216390_10386; -.
DR   Proteomes; UP000198626; 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; 2.60.40.1080; -; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000198626};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..1068
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039442194"
FT   DOMAIN          945..1063
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          40..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1068 AA;  115401 MW;  14EE9CF627B96CA7 CRC64;
     MRKKYNGFLA LLLSASMIFG GSGVSTVNAY GAETGISEDS ISTEVVETEA SESTEEAKIE
     EASKESTEEV SEDSVETEST KEVSEDEVTT ESANATTSTN AAETTAKTAA TGSLSDWDYP
     TRSYTYDGKG VTFSENTKLK TASDSYTYKY YYSTSSNQAD KNEVSKTGLV DAGWYVISAN
     AISDGNVVSS VSFDYIIKPA PLTVSTADAE ATVTNESGKL DTPLQAKDAS IISGSVVSGD
     KIEFTDWASI DKVGVSENSC TAVGADNTKI SNYEITYKFG TLTVLSGWDS DRNQMNNIRN
     LNATMNKKGV VTVKWAQPKK AKRVTYSVYR RNTDGTWTRL TEGIKKKSYK DTDAMNVVSS
     GEGQLVYRVI ARGTDTYGQE GSGAPAYVQC VPKILTFESG PNYKYINLKF VSNEAPAGYQ
     IEQFSTKNKS KKDVITVSSS DLKAEVYTGK VVKNKNATIT AVNYKDEGSE NVTIANSKNV
     KFTFRIAAAP FTISDLGETV EIPQSKYTGK KSVKLTTGSC PQVTASADSL TQINFTYSKV
     KKAKGYLVEY STSPDFTTSN NNIYVKAFIT AKTSDSTYKK WKVGYYDDMP NAGKIVVNNV
     VTGVPYYFRC TAYFNFKPTS DYDTVDGDPG VTSDVVMNYG RPVGVTSLTA KYYDGTKSDA
     GLTWNYTTKY GDNIIGYRVT RQNYKENTSS KEFTVEDGAL VELRGLANRN KEKSYKVADS
     NKIPNGERIE YTVQAIYQNV NSNFKATGSN IIYSDPVTVD YMNPTGIEFL KSASSSSKKK
     KKSTSTATSY TVTKGGTLNV SKLLKFDPES TTNKEVDYAS SNTEYFKVSK DGVITGVKNT
     GSKTVTLTVT SKNDSNVSND IQIKVGSATS SSGGSSGSGS DTSSLVVCLD PGHGGSDSGT
     TNGSVKEKDV NLAIAKKVGE YLEDEGVKVY YTRSTDTYIS LTDRTDYAQD KGCNLFVSIH
     CNSGSSSAKG TEVYYSLTKY GRKNLASKIS SAVATALDTT NRGAKTRQGD NGDYYSVIRT
     SAAKGIPGLI VEHGYLSNSS DLAKLTNSNY VKAAAKAEAN AIVKYWKS
//
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