EXLYS_BPKMV
ID EXLYS_BPKMV Reviewed; 898 AA.
AC Q7Y2C9;
DT 29-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 23-FEB-2022, entry version 74.
DE RecName: Full=Peptidoglycan hydrolase gp36 {ECO:0000305};
DE EC=3.2.1.17 {ECO:0000312|EMBL:CAD44227.1};
DE AltName: Full=Gene product 36 {ECO:0000305};
DE Short=Gp36;
GN Name=gp36 {ECO:0000312|EMBL:CAD44227.1};
OS Pseudomonas phage phiKMV.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Krylovirinae; Phikmvvirus.
OX NCBI_TaxID=204270 {ECO:0000312|Proteomes:UP000000842};
OH NCBI_TaxID=287; Pseudomonas aeruginosa.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12890620; DOI=10.1016/s0042-6822(03)00123-5;
RA Lavigne R., Burkal'tseva M.V., Robben J., Sykilinda N.N., Kurochkina L.P.,
RA Grymonprez B., Jonckx B., Krylov V.N., Mesyanzhinov V.V., Volckaert G.;
RT "The genome of bacteriophage phiKMV, a T7-like virus infecting Pseudomonas
RT aeruginosa.";
RL Virology 312:49-59(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, IDENTIFICATION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15549178; DOI=10.1007/s00018-004-4301-y;
RA Lavigne R., Briers Y., Hertveldt K., Robben J., Volckaert G.;
RT "Identification and characterization of a highly thermostable bacteriophage
RT lysozyme.";
RL Cell. Mol. Life Sci. 61:2753-2759(2004).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND FUNCTION.
RX PubMed=16847574; DOI=10.1007/s00018-006-6183-7;
RA Briers Y., Lavigne R., Plessers P., Hertveldt K., Hanssens I.,
RA Engelborghs Y., Volckaert G.;
RT "Stability analysis of the bacteriophage phiKMV lysin gp36C and its
RT putative role during infection.";
RL Cell. Mol. Life Sci. 63:1899-1905(2006).
RN [4]
RP REVIEW.
RX PubMed=22991936; DOI=10.3109/1040841x.2012.723675;
RA Rodriguez-Rubio L., Martinez B., Donovan D.M., Rodriguez A., Garcia P.;
RT "Bacteriophage virion-associated peptidoglycan hydrolases: potential new
RT enzybiotics.";
RL Crit. Rev. Microbiol. 39:427-434(2013).
CC -!- FUNCTION: Component of the cylindrical core that assembles on the inner
CC surface of the capsid during procapsid formation. Plays a role in
CC ejection of the bacteriophage DNA into the host cell at the initiation
CC of infection. Functions as an exolysin that catalyzes the cleavage of
CC the host peptidoglycans. {ECO:0000305|PubMed:15549178,
CC ECO:0000305|PubMed:16847574}.
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:0000312|EMBL:CAD44227.1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:16847574};
CC Temperature dependence:
CC The enzyme is highly thermoresistant, but not thermostable.
CC {ECO:0000269|PubMed:16847574};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:15549178}.
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DR EMBL; AJ505558; CAD44227.1; -; Genomic_DNA.
DR RefSeq; NP_877475.1; NC_005045.1.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR GeneID; 1482616; -.
DR KEGG; vg:1482616; -.
DR Proteomes; UP000000842; Genome.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0098932; P:disruption by virus of host cell wall peptidoglycan during virus entry; IEA:UniProtKB-KW.
DR GO; GO:0044409; P:entry into host; IDA:UniProtKB.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0099002; P:viral genome ejection through host cell envelope, short tail mechanism; IEA:UniProtKB-KW.
DR Gene3D; 1.10.530.40; -; 1.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR023347; Lysozyme_dom_sf.
DR SUPFAM; SSF53955; SSF53955; 1.
PE 1: Evidence at protein level;
KW Antimicrobial; Bacteriolytic enzyme;
KW Degradation of host cell envelope components during virus entry;
KW Degradation of host peptidoglycans during virus entry; Glycosidase;
KW Hydrolase; Reference proteome;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Viral short tail ejection system;
KW Virion; Virus entry into host cell.
FT CHAIN 1..898
FT /note="Peptidoglycan hydrolase gp36"
FT /id="PRO_0000432973"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 898 AA; 98250 MW; 0114C0EBE1657D3C CRC64;
MAESQRASQE LGINVGQTQL QPGQSARRGV RDSEVNYSGP SVGSQILDGI LGAGQQIAGK
WFEHNVQQEV LRGERARMAG EAEEAVDSNV LAKPFVKGGW RKQDYRIAQA DFSLKMQRFI
ANKGREMTPE EFRKYLSQEA THVLDSTEGM NPNDALQALA QQQKAEEQLF GMQAKAYMDW
SIDQAARGFR TQGNSILAKA VQAQATGDEL SRQLSLEEAG LFYTNIMTSE DIPLEVRDKV
GMQFLAASLD MNQRGIYEGL RDAGFLDSMS FDDRRALNGL YEKSKAQTRA KESMATLRAD
ADFQQRVANG AITDLAEVEA YSRGMVEEGR WSDAQAISFM TKAMTGLGNA QRMQGIMAAL
EAGDINALHT LGTNVTEALE QWDKMQAANG SSLTDRLVQG TQLGLRLGTF PKTYGESVGS
AVRMIQAAKE GEANPELVNT LNSIFEQVAS AQEINPSAGN VMLSGIPEAE QGAVAWALKQ
MKMGIAPAQA LREFSANAEV VKQMDEFEKG QNTKAFKDNL GKQVNDKFVN NIFGRAWNML
TGESDLSNNE AVLSMYRRAT IDEANWLASD RKHAGLLTSD TGREALLEIA AANVRNRTIQ
VGEGRNLKEG DLFSRRDSAP LILPRGTTAE QLFGTNDTET IGTVLAEQHK PHVEGLLGYK
SVVAFEYDRT SGSLLAVEYD ENGVALDRTR VDPQAVGKEV LKRNADKLNA MRGAEYGANV
KVSGTDIRMN GGNSAGMLKQ DVFNWRKELA QFEAYRGEAY KDADGYSVGL GHYLGSGNAG
AGTTVTPEQA AQWFAEDTDR ALDQGVRLAD ELGVTNNASI LGLAGMAFQM GEGRARQFRN
TFQAIKDRNK EAFEAGVRNS KWYTQTPDRA EAFIKRMAPH FDTPSQIGVD WYSAATAE
