ID DEPOL_BPKRA Reviewed; 907 AA. AC P0DTN8; DT 13-SEP-2023, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2023, sequence version 1. DT 27-MAR-2024, entry version 3. DE RecName: Full=Depolymerase, capsule K2-specific {ECO:0000305}; DE Short=DpK2 {ECO:0000303|PubMed:34431721}; DE AltName: Full=Gene product 2; DE Short=gp2 {ECO:0000305}; DE AltName: Full=Tail spike protein {ECO:0000303|PubMed:34431721}; GN OrderedLocusNames=RAD2_02; OS Klebsiella phage RAD2 (Bacteriophage RAD2). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Drexlerviridae; Webervirus. OX NCBI_TaxID=2831671; OH NCBI_TaxID=573; Klebsiella pneumoniae. RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], STRUCTURE BY ELECTRON MICROSCOPY (2.70 RP ANGSTROMS), SUBCELLULAR LOCATION, FUNCTION, SUBUNIT, AND DOMAIN. RX PubMed=34431721; DOI=10.1128/spectrum.01023-21; RA Dunstan R.A., Bamert R.S., Belousoff M.J., Short F.L., Barlow C.K., RA Pickard D.J., Wilksch J.J., Schittenhelm R.B., Strugnell R.A., Dougan G., RA Lithgow T.; RT "Mechanistic Insights into the Capsule-Targeting Depolymerase from a RT Klebsiella pneumoniae Bacteriophage."; RL Microbiol. Spectr. 9:e0102321-e0102321(2021). RN [2] RP REVIEW. RX PubMed=31803168; DOI=10.3389/fmicb.2019.02649; RA Latka A., Leiman P.G., Drulis-Kawa Z., Briers Y.; RT "Modeling the Architecture of Depolymerase-Containing Receptor Binding RT Proteins in Klebsiella Phages."; RL Front. Microbiol. 10:2649-2649(2019). CC -!- FUNCTION: Constitutes the tail fiber, which functions as a receptor CC binding protein (RBP) and mediates the attachment to the host capsular CC exopolysaccharides (PubMed:34431721). Displays a depolymerase activity CC that specifically degrades the K2-type polysaccharides of Klebsiella CC pneumoniae, which allows the phage to reach the host cell membrane and CC bind the entry receptor (PubMed:34431721). CC {ECO:0000269|PubMed:34431721}. CC -!- SUBUNIT: Homotrimer. {ECO:0000305|PubMed:34431721}. CC -!- SUBCELLULAR LOCATION: Virion. Note=Tail appendage. Forms globular CC appendages on the phage virion tail tip. {ECO:0000269|PubMed:34431721}. CC -!- DOMAIN: The N-terminus contains an extended triple helical bundle CC (PubMed:34431721). The central part is a beta-helical domain, which CC forms a negatively charged cavity at the interface between neighboring CC monomers (PubMed:34431721). This cavity may contain the active site CC (PubMed:34431721). The C-terminus is formed by 3 four-stranded beta- CC sandwich folds (PubMed:34431721). {ECO:0000269|PubMed:34431721}. CC -!- SIMILARITY: In the N-terminal section; belongs to the Webervirus CC depolymerase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the K2-specific CC depolymerase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MW655991; QUU29414.1; -; Genomic_DNA. DR PDB; 7LZJ; EM; 2.70 A; A/B/C=1-907. DR PDBsum; 7LZJ; -. DR SMR; P0DTN8; -. DR GO; GO:0098024; C:virus tail, fiber; IEA:UniProtKB-KW. DR GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW. DR GO; GO:0098994; P:disruption of host cell envelope during viral entry; IEA:UniProtKB-KW. DR GO; GO:0098996; P:disruption of host cell glycocalyx during viral entry; IDA:UniProtKB. DR Gene3D; 6.10.140.1630; -; 1. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR SUPFAM; SSF51126; Pectin lyase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Degradation of host capsule during virus entry; KW Degradation of host cell envelope components during virus entry; KW Host-virus interaction; Viral attachment to host adhesion receptor; KW Viral attachment to host cell; Viral tail fiber protein; KW Viral tail protein; Virion; Virus entry into host cell. FT CHAIN 1..907 FT /note="Depolymerase, capsule K2-specific" FT /id="PRO_0000458739" FT REGION 137..169 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 907 AA; 98355 MW; 50D98EB43856BF21 CRC64; MALYREGKAA MAADGTVTGT GTKWQSSLSL IRPGATIMFL SSPIQMAVVN KVVSDTEIKA ITTSGAVVAS TDYAILLSDS LTVDGLAQDV AETLRHYQSQ ETVIADAVEF FKSFDFDSLQ NLANQIKADS ESAESSAAAA AASESKAKTS EDNAKSSENA AKNSEVAAET TRDQIQQIID NAGDQSTLVV LAQPDGFDSI GRVSSFAALR NLKPKKSGQH VLLTSYYDGW AAENKMPTGG GEFISSIGTA TDDGGYIAAG PGYYWTRVVN NNSFTAEDFG CKTTATPPPN FNVLPAELFD NTAMMQAAFN LAISKSFKLN LSTGTYYFES SDTLRITGPI HIEGRPGTVF YHNPSNKANP KTDAFMNISG CSAGRISSIN CFSNSYLGKG INFDRSVGDN RKLVLEHVYV DTFRWGFYVG EPECINQIEF HSCRAQSNYF QGIFIESFKE GQEYGHSAPV HFFNTICNGN GPTSFALGAT YKTTKNEYIK VMDSVNDVGC QAYFQGLSNV QYIGGQLSGH GSPRNTSLAT ITQCNSFIIY GTDLEDINGF TTDGTAITAD NIDAIESNYL KDISGAAIVV SSCPGFKIDS PHIFKIKTLS TIKLMNNTYN YEIGGFTPDE ALKYNVWDAN GLATNRISGV IHPRLVNSRL GINSVAFDNM SNKLDVSSLI HNETSQIVGL TPSTGSNVPH TRKMWSNGAM YSSTDLNNGF RLNYLSNHNE PLTPMHLYNE FSVSEFGGSV TESNALDEIK YIFIQTTYAN SGDGRFIIQA LDASGSVLSS NWYSPQSFNS TFPISGFVRF DVPTGAKKIR YGFVNSANYT GSLRSHFMSG FAYNKRFFLK IYAVYNDLGR YGQFEPPYSV AIDRFRVGDN TTQMPSIPAS SATDVAGVNE VINSLLASLK ANGFMSS //