ID   A9MN07_SALAR            Unreviewed;      1032 AA.
AC   A9MN07;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Lysozyme {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|RuleBase:RU003788};
DE            EC=3.2.1.17 {ECO:0000256|ARBA:ARBA00012732, ECO:0000256|RuleBase:RU003788};
GN   OrderedLocusNames=SARI_02625 {ECO:0000313|EMBL:ABX22482.1};
OS   Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=41514 {ECO:0000313|EMBL:ABX22482.1, ECO:0000313|Proteomes:UP000002084};
RN   [1] {ECO:0000313|EMBL:ABX22482.1, ECO:0000313|Proteomes:UP000002084}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980
RC   {ECO:0000313|Proteomes:UP000002084};
RG   The Salmonella enterica serovar Arizonae Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) 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         ECO:0000256|RuleBase:RU003788};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC       {ECO:0000256|RuleBase:RU003788}.
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DR   EMBL; CP000880; ABX22482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9MN07; -.
DR   STRING; 41514.SARI_02625; -.
DR   CAZy; GH24; Glycoside Hydrolase Family 24.
DR   KEGG; ses:SARI_02625; -.
DR   HOGENOM; CLU_010665_1_2_6; -.
DR   Proteomes; UP000002084; Chromosome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
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; cd00737; lyz_endolysin_autolysin; 1.
DR   CDD; cd12797; M23_peptidase; 1.
DR   Gene3D; 1.10.530.40; -; 1.
DR   Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR   HAMAP; MF_04110; ENDOLYSIN_T4; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR033907; Endolysin_autolysin.
DR   InterPro; IPR034690; Endolysin_T4_type.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR023347; Lysozyme_dom_sf.
DR   PANTHER; PTHR38107; -; 1.
DR   PANTHER; PTHR38107:SF3; LYSOZYME RRRD-RELATED; 1.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Antimicrobial {ECO:0000256|ARBA:ARBA00022529,
KW   ECO:0000256|RuleBase:RU003788};
KW   Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638,
KW   ECO:0000256|RuleBase:RU003788};
KW   Glycosidase {ECO:0000256|RuleBase:RU003788};
KW   Host cytoplasm {ECO:0000256|ARBA:ARBA00023200};
KW   Hydrolase {ECO:0000256|RuleBase:RU003788};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002084}.
FT   DOMAIN          558..588
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
SQ   SEQUENCE   1032 AA;  115439 MW;  99C3326F2257E9F2 CRC64;
     MTAKMPKISF PVPSNKNGHP FSSAEELLSA LGGESSGLYL VGSQGMWHGG IHITDATMPW
     CALSTDSAAE SEYRPELYKG EQFIRCMADG EIVAWRVCES YESAGIDWRG EKLLLSNSFV
     LVKHYIQPGD SVESGLTFFT LYMNMAPYLA YKQQGNQLDR KVAGVQRYYT SVEDLQAGHV
     TGKLEKDTVV TLSDTIVTRS SDKRQFTEVT ITSETKNAAG NTLAAGTKVW TVSDQGSLKV
     AASAPVPSWW TKCSPAYTNQ SESVVNCTSR TNWAYYLSSD DVLQYKNAGS LVADFPLSYE
     PDNTAQQVIR PGKNAGDAER TFSLVTLGRD KDKLKKDDRV WVVSDGDSLT PVAPAASSSE
     PVFNGVYVPP TPVPVSAGDS LGHLGFYQLP EENGKRSRYQ VHIECLSMDD MEKFITNPGR
     VGEDTPVYLT WQADAPLFEK GEQGMVAGSR KTKISGIVTL AKVPGVDAAG TALSDNKDAA
     YFQIRQEGGW LPTASVQKVS QYALGELGFA TLDKAPASFD LIDGINQPNN VVKGILEQLY
     KAAQEETRTT HALNKYNYKR LLELIDRNQD GYYSEQEYLQ AIHNVSYRDH LYRVIAKHAS
     EWYYGKDAPL WKTYLDTLTT DAPLWKMYLE TFLDKMTWMK AVSEKGVPLG PAPWHMHPIV
     FMDSLSQKKT HQIIFPLKVK PKNDKRGIWK DYYWAAALSD SNASQSIFGR NRDSGRRKHA
     ARDLYTEPRA EIVAICAGVV KSISTYYYGT WQITIEHKTN DGREFFIRYG EVEHNSIIVN
     VGDRVLLGSV IARTGLLINP RTQRHPNIIP GQIVYMLHLE YYTNMSEGVP PNNTGGTVTP
     YDRRSDLQDP LDILREGYKN TFEQDDANER IDINQLNISE QGKQFIKEWE GLRTEAYNDS
     EGYCTIGYGH LIARDRCESI TLPDEFSHGI TQERANELFE ERLPSYVDGV KSSVSVKLYQ
     YEFDALVCLL FNIGSSGLRL KAPMLRNKLN QEDYEGAAQE FLDITNGGES GLVARRISEN
     NLFLNNIYDA SH
//