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Database: UniProt
Entry: A0A1W9PFV6_9HELI
LinkDB: A0A1W9PFV6_9HELI
Original site: A0A1W9PFV6_9HELI 
ID   A0A1W9PFV6_9HELI        Unreviewed;       460 AA.
AC   A0A1W9PFV6;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN   ORFNames=B5M52_07750 {ECO:0000313|EMBL:OQX57294.1};
OS   Helicobacteraceae bacterium 4484_230.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae.
OX   NCBI_TaxID=1968531 {ECO:0000313|EMBL:OQX57294.1, ECO:0000313|Proteomes:UP000192641};
RN   [1] {ECO:0000313|Proteomes:UP000192641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) 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:OQX57294.1}.
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DR   EMBL; MZGN01000124; OQX57294.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9PFV6; -.
DR   Proteomes; UP000192641; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..460
FT                   /note="MurNAc-LAA domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013162483"
FT   DOMAIN          299..453
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          95..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        95..111
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  52103 MW;  795D44DA5091E46A CRC64;
     MLRFFVSVIV FAALCFAGTD AELLKHADAN LKSSSKNDQF KAYDTYKQVY LKALVEGNDK
     VCKRCLQGIV TSGRMLHIDV DKYSKKLSKY KQAPSKKTVV HRKKKSRTKT ASGKNIKLSS
     QRALESVQWN GGDLVLAFDS PLKAKDVNYF SIQEKKKRRF RYIFDIHSIQ TKNHTIKHRE
     IKRIKLGQYK SGTLRLVIES TKKLPLHFKL DNELLVIMLG VKRVKAPLAN KPMHAKNKTI
     VIDPGHGGKD AGAVGYKRYF EKNVVLQIAK KFAEILKKDG YKVYMTRSSD KFISLRQRTA
     FANRKKADLF ISIHANAVPK KNTKKAHGIE TYFLSTARSG RAERIAAKEN AVDMRGFKGG
     QKGYLEGMTN RKTIASHKLA IDIQQGILSK MRAHYSDVKD GGVRGGPFWV LVGAQMPSVL
     VEVGFISHPK EARRLVNRRY QKYFAQSLAD GVNRYFSKNP
//
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