ID A0A093JAW0_FULGA Unreviewed; 212 AA.
AC A0A093JAW0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Lysozyme g {ECO:0000256|ARBA:ARBA00016485};
DE EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732};
DE AltName: Full=1,4-beta-N-acetylmuramidase {ECO:0000256|ARBA:ARBA00031262};
DE Flags: Fragment;
GN ORFNames=N327_10614 {ECO:0000313|EMBL:KFW12170.1};
OS Fulmarus glacialis (Northern fulmar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Procellariiformes; Procellariidae;
OC Fulmarus.
OX NCBI_TaxID=30455 {ECO:0000313|EMBL:KFW12170.1, ECO:0000313|Proteomes:UP000053806};
RN [1] {ECO:0000313|EMBL:KFW12170.1, ECO:0000313|Proteomes:UP000053806}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N327 {ECO:0000313|EMBL:KFW12170.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic
CC acid and N-acetyl-D-glucosamine residues in a peptidoglycan and
CC between N-acetyl-D-glucosamine residues in chitodextrins.;
CC EC=3.2.1.17; Evidence={ECO:0000256|ARBA:ARBA00000632};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 23 family.
CC {ECO:0000256|ARBA:ARBA00008902}.
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DR EMBL; KK611028; KFW12170.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093JAW0; -.
DR Proteomes; UP000053806; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd01021; GEWL; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR InterPro; IPR002152; Glyco_hydro_23.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR31698:SF8; LYSOZYME G; 1.
DR PANTHER; PTHR31698; LYSOZYME G FAMILY MEMBER; 1.
DR Pfam; PF01464; SLT; 1.
DR PIRSF; PIRSF001065; Lysozyme_g; 1.
DR PRINTS; PR00749; LYSOZYMEG.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000053806};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..212
FT /note="Lysozyme g"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001885394"
FT DOMAIN 77..186
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
FT ACT_SITE 99
FT /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
FT ACT_SITE 112
FT /evidence="ECO:0000256|PIRSR:PIRSR001065-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFW12170.1"
FT NON_TER 212
FT /evidence="ECO:0000313|EMBL:KFW12170.1"
SQ SEQUENCE 212 AA; 23377 MW; 1DA74CF88CCBB545 CRC64;
VLRKNQAMYP MLVLLGLAAL LGASQGRTDC YGSVNRIKTP GASCKTAKPE GLSYCGVRAS
EKIAERDLRA MDQYKTLIKK VGEKLCIEPA LIAGIISRES HAGKILRNGW GDNGNGFGLM
QVDKKSGHTP VGRWNSEAHL TQGTNILIAM IKTIQRNFPR WTKDQQLKGG ISAYNAGSKN
VRSYDRMDIG TTHNDYSNDV VARAQYYKKH GY
//
