ID D5JFK5_9CAUD Unreviewed; 589 AA.
AC D5JFK5;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=Pre-baseplate central spike protein {ECO:0000256|HAMAP-Rule:MF_04151};
DE AltName: Full=Peptidoglycan hydrolase {ECO:0000256|HAMAP-Rule:MF_04151};
DE EC=3.2.1.17 {ECO:0000256|HAMAP-Rule:MF_04151};
DE Contains:
DE RecName: Full=Mature baseplate central spike protein {ECO:0000256|HAMAP-Rule:MF_04151};
DE Contains:
DE RecName: Full=Baseplate central spike protein C-terminus {ECO:0000256|HAMAP-Rule:MF_04151};
GN ORFNames=KP15_157 {ECO:0000313|EMBL:ADE34988.1};
OS Klebsiella phage KP15.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Slopekvirus; Slopekvirus kp15.
OX NCBI_TaxID=707757 {ECO:0000313|EMBL:ADE34988.1, ECO:0000313|Proteomes:UP000002373};
RN [1] {ECO:0000313|EMBL:ADE34988.1, ECO:0000313|Proteomes:UP000002373}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Drulis-Kawa Z., Maciaszczyk-Dziubinska E., Bocer T.;
RT "Genomic sequence and analysis of Klebsiella sp. KP15 bacteriophage.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: [Mature baseplate central spike protein]: Baseplate central
CC spike complex-associated lysozyme that is essential for the localized
CC hydrolysis of bacterial cell wall, so that the tail tube, through which
CC the phage DNA is ejected, can penetrate to the host inner membrane. The
CC tail lysozyme complex at the tip of the tail tube penetrates through
CC the outer membrane into the periplasm. This way, lysozyme domain is
CC released and locally digests the peptidoglycan layer to make a hole to
CC let the tube penetrate to the inner membrane. Involved in the tail
CC assembly. {ECO:0000256|HAMAP-Rule:MF_04151}.
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|HAMAP-Rule:MF_04151, ECO:0000256|RuleBase:RU003788};
CC -!- SUBUNIT: [Baseplate central spike protein C-terminus]: Homotrimer. The
CC central spike complex creates an extension of the tail tube.
CC {ECO:0000256|HAMAP-Rule:MF_04151}.
CC -!- SUBUNIT: [Mature baseplate central spike protein]: Monomer. The central
CC spike complex creates an extension of the tail tube.
CC {ECO:0000256|HAMAP-Rule:MF_04151}.
CC -!- SUBUNIT: [Pre-baseplate central spike protein]: Homotrimer.
CC {ECO:0000256|HAMAP-Rule:MF_04151}.
CC -!- SUBCELLULAR LOCATION: [Mature baseplate central spike protein]: Virion
CC {ECO:0000256|HAMAP-Rule:MF_04151}. Note=Present in the baseplate.
CC {ECO:0000256|HAMAP-Rule:MF_04151}.
CC -!- SUBCELLULAR LOCATION: [Pre-baseplate central spike protein]: Virion
CC {ECO:0000256|HAMAP-Rule:MF_04151}. Note=Present in the baseplate.
CC {ECO:0000256|HAMAP-Rule:MF_04151}.
CC -!- SUBCELLULAR LOCATION: [Baseplate central spike protein C-terminus]:
CC Virion {ECO:0000256|HAMAP-Rule:MF_04151}. Note=Present in the
CC baseplate. {ECO:0000256|HAMAP-Rule:MF_04151}.
CC -!- PTM: [Pre-baseplate central spike protein]: In the fully assembled
CC virus, the pre-baseplate central spike protein is cleaved to form the
CC mature baseplate central spike protein, and a C-terminus fragment, the
CC baseplate central spike protein C-terminus. The two fragments remain
CC associated with the virion. {ECO:0000256|HAMAP-Rule:MF_04151}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC {ECO:0000256|HAMAP-Rule:MF_04151, ECO:0000256|RuleBase:RU003788}.
CC -!- CAUTION: The cleavage site between the mature baseplate central spike
CC protein and the baseplate central spike protein C-terminus is
CC uncertain. {ECO:0000256|HAMAP-Rule:MF_04151}.
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DR EMBL; GU295964; ADE34988.1; -; Genomic_DNA.
DR RefSeq; YP_003580033.1; NC_014036.1.
DR CAZy; GH24; Glycoside Hydrolase Family 24.
DR GeneID; 8997389; -.
DR KEGG; vg:8997389; -.
DR Proteomes; UP000002373; Genome.
DR GO; GO:0098025; C:virus tail, baseplate; IEA:UniProtKB-UniRule.
DR GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-UniRule.
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:0098932; P:disruption by virus of host cell wall peptidoglycan during virus entry; IEA:UniProtKB-UniRule.
DR GO; GO:0098994; P:disruption of host cell envelope during viral entry; 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:UniProtKB-UniRule.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-UniRule.
DR CDD; cd00735; T4-like_lys; 1.
DR Gene3D; 1.10.530.40; -; 1.
DR Gene3D; 3.10.450.190; -; 1.
DR Gene3D; 2.40.50.260; Nucleic acid-binding protein domain; 1.
DR HAMAP; MF_04151; NEEDLE_T4; 1.
DR InterPro; IPR002196; Glyco_hydro_24.
DR InterPro; IPR010609; Gp5_C.
DR InterPro; IPR009590; Gp5_OB_N.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR023347; Lysozyme_dom_sf.
DR InterPro; IPR046397; NEEDLE_T4.
DR InterPro; IPR001165; T4-type_lysozyme.
DR PANTHER; PTHR37406; T4-TYPE LYSOZYME 1-RELATED; 1.
DR PANTHER; PTHR37406:SF1; T4-TYPE LYSOZYME 1-RELATED; 1.
DR Pfam; PF06715; Gp5_C; 1.
DR Pfam; PF06714; Gp5_OB; 1.
DR Pfam; PF00959; Phage_lysozyme; 1.
DR PRINTS; PR00684; T4LYSOZYME.
DR SUPFAM; SSF69255; gp5 N-terminal domain-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF69349; Phage fibre proteins; 1.
PE 3: Inferred from homology;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022529, ECO:0000256|HAMAP-
KW Rule:MF_04151};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638, ECO:0000256|HAMAP-
KW Rule:MF_04151};
KW Degradation of host cell envelope components during virus entry
KW {ECO:0000256|HAMAP-Rule:MF_04151};
KW Degradation of host peptidoglycans during virus entry {ECO:0000256|HAMAP-
KW Rule:MF_04151};
KW Glycosidase {ECO:0000256|HAMAP-Rule:MF_04151,
KW ECO:0000256|RuleBase:RU003788};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04151, ECO:0000256|RuleBase:RU003788};
KW Late protein {ECO:0000256|HAMAP-Rule:MF_04151};
KW Viral baseplate protein {ECO:0000256|HAMAP-Rule:MF_04151};
KW Viral genome ejection through host cell envelope {ECO:0000256|HAMAP-
KW Rule:MF_04151};
KW Viral penetration into host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04151};
KW Viral release from host cell {ECO:0000256|ARBA:ARBA00022612,
KW ECO:0000256|HAMAP-Rule:MF_04151};
KW Viral tail assembly {ECO:0000256|HAMAP-Rule:MF_04151};
KW Viral tail protein {ECO:0000256|HAMAP-Rule:MF_04151};
KW Virion {ECO:0000256|HAMAP-Rule:MF_04151};
KW Virus entry into host cell {ECO:0000256|HAMAP-Rule:MF_04151}.
FT CHAIN 1..589
FT /note="Pre-baseplate central spike protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04151"
FT /id="PRO_5035346498"
FT CHAIN 1..354
FT /note="Mature baseplate central spike protein"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04151"
FT /id="PRO_5035346499"
FT CHAIN 355..589
FT /note="Baseplate central spike protein C-terminus"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04151"
FT /id="PRO_5035346500"
FT DOMAIN 34..174
FT /note="Protein Gp5 N-terminal OB-fold"
FT /evidence="ECO:0000259|Pfam:PF06714"
FT ACT_SITE 188
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04151"
FT ACT_SITE 197
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04151"
FT SITE 354..355
FT /note="Cleavage"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04151"
SQ SEQUENCE 589 AA; 64376 MW; A7A300D7545DACF1 CRC64;
MKLGGNLHSP FFDGVVENVD DPRGLGRVQV RVFGQHPAQK QKSDAIGVPV EDLPWMMPIQ
DIRSAAISGV GFSPTGITRG SFVVGYWRDK WHQDGMIIGT VAGEYVEQPD TQKGFCDPMG
EYPRYVGNDV NSLALGGLKG KGSSSVIIRD SNTIIAVNPD DRPLDEIPED NRPDTGGFTI
EKMLKQDEGI RTRWYTDSEG YPTIGIGHLL IREKTRDTAK INAAISKAVG REVTNGTITA
EEVSTLFAQD LAKVRSDIQR TANVREVYVN LNRPRQMAIE NMSFQMGVGG VAKFTNTLKA
MKNEDWQAAY NGLRNSLWAS QTPGRSSRVS KIVLTGNLES YGVQVPDPEG RSLSAAYAAY
NGATLSATSP EDPFTPGDTR VMFEEPASSY NAEYPYNMVF ESRSGHIQEF DDTPGYERYN
RVHPAGSYEE IRPDGTRVVK IVGDDYQIVM QGRKLNVKGN LQVVIEGDAF IYNMGNVQQT
VDGNVTEFVR GNVQQTVEGE YVGLIKGNAE LTVNKDATVN VDQNLTANVK QNATVAVTED
ATITAKNAKM EIEETMDIGA KDINIKATNN TFIDSGALTK ITGGTVQVG
//
