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 02-OCT-2024, entry version 5. 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:symbiont entry into host cell via disruption of host cell envelope; IEA:UniProtKB-KW. DR GO; GO:0098996; P:symbiont entry into host cell via disruption of host cell glycocalyx; 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" FT HELIX 196..199 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 206..210 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7LZJ" FT TURN 230..234 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 241..248 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 254..260 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 263..267 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 276..279 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 302..314 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 318..320 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 323..328 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 334..336 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 348..352 FT /evidence="ECO:0007829|PDB:7LZJ" FT TURN 360..362 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 364..368 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 375..382 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 388..393 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 404..419 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 421..425 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 429..437 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 439..447 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 461..464 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 466..469 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 474..477 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 488..491 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 501..514 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 516..518 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 528..533 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 535..541 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 543..550 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 562..568 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 569..573 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 575..582 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 587..589 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 593..607 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 621..623 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 625..628 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 639..641 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 643..645 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 647..650 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 654..658 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 663..665 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 669..674 FT /evidence="ECO:0007829|PDB:7LZJ" FT TURN 703..705 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 710..712 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 726..732 FT /evidence="ECO:0007829|PDB:7LZJ" FT TURN 742..744 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 748..757 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 763..771 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 773..775 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 777..781 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 785..787 FT /evidence="ECO:0007829|PDB:7LZJ" FT TURN 792..794 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 795..801 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 808..819 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 823..826 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 828..836 FT /evidence="ECO:0007829|PDB:7LZJ" FT STRAND 838..847 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 863..866 FT /evidence="ECO:0007829|PDB:7LZJ" FT HELIX 888..901 FT /evidence="ECO:0007829|PDB:7LZJ" 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 //