ID DPOL2_BPK52 Reviewed; 685 AA. AC A0A219YHC2; DT 13-SEP-2023, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2017, sequence version 1. DT 08-NOV-2023, entry version 23. DE RecName: Full=Depolymerase 2, capsule K5-specific {ECO:0000305}; DE AltName: Full=Gene product 38 {ECO:0000305}; DE Short=gp38 {ECO:0000305}; DE AltName: Full=K5 depolymerase; DE AltName: Full=Probable tail spike protein {ECO:0000305}; GN ORFNames=k52_038 {ECO:0000312|EMBL:APZ82805.1}; OS Klebsiella phage K5-2 (Bacteriophage K5-2). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Autographiviridae; Studiervirinae; Przondovirus; Przondovirus K52. OX NCBI_TaxID=1932361; OH NCBI_TaxID=570; Klebsiella. RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND FUNCTION. RX PubMed=28676686; DOI=10.1038/s41598-017-04644-2; RA Hsieh P.F., Lin H.H., Lin T.L., Chen Y.Y., Wang J.T.; RT "Two T7-like Bacteriophages, K5-2 and K5-4, Each Encodes Two Capsule RT Depolymerases: Isolation and Functional Characterization."; RL Sci. Rep. 7:4624-4624(2017). 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: Functions as a receptor binding protein (RBP) and probably CC mediates the attachment to the host capsular exopolysaccharides CC (Probable). Displays a depolymerase activity that specifically degrades CC the K5-type polysaccharides of Klebsiella pneumoniae capsule, which CC allows the phage to reach the host cell membrane and bind the entry CC receptor (PubMed:28676686). {ECO:0000269|PubMed:28676686, CC ECO:0000305|PubMed:28676686}. CC -!- SUBUNIT: Homotrimer. Interacts (via N-terminus) with depolymerase 1 CC (via N-terminus); this interaction probably gives rise to a branched CC tailspike. {ECO:0000250|UniProtKB:D1L2X1}. CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:D1L2X1}. Note=Tail CC appendage. Depolymerase 1 is connected to the phage tail via an N- CC terminal anchor domain, while depolymerase 2 is attached to CC depolymerase 1. {ECO:0000250|UniProtKB:D1L2X1}. CC -!- SIMILARITY: In the N-terminal section; belongs to the Przondovirus CC depolymerase 2 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; KY389315; APZ82805.1; -; Genomic_DNA. DR Proteomes; UP000224375; Genome. DR GO; GO:0098015; C:virus tail; 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; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1. DR InterPro; IPR012334; Pectin_lyas_fold. PE 3: Inferred from homology; KW Degradation of host capsule during virus entry; KW Degradation of host cell envelope components during virus entry; KW Host-virus interaction; Reference proteome; KW Viral attachment to host adhesion receptor; Viral attachment to host cell; KW Viral tail protein; Virion; Virus entry into host cell. FT CHAIN 1..685 FT /note="Depolymerase 2, capsule K5-specific" FT /id="PRO_0000458714" SQ SEQUENCE 685 AA; 71412 MW; CFCA3BE6B47EB5B8 CRC64; MIKNDFNQPK GSTIGVLKDG RTIQEAFDSL GYLGVAVLSP ANYGAKGDGK ADDTIPLRQC VQDACALGGR VVGTVGAEYK ISGTIAGTVG DGKYVELDFT GSKFVPTTDD AVMTITGVAT SPVAEVTVEV VSVNLGNGST NTIAMKVTAP GGHSFTKKGE IGKAWSPVLC LNNDLSTQYA GEPFVVGLVE SSTVFYTTSV FTELYMGTSL KVIRVPTTQV VVKGLDVESE WTTGWKASTL TLSGLLRPFV YKPKCKNING PFVNLTGCYG ATVFLPEGDN LRNAPSEGAY GYFVNDSASF GSTIYGINCT NARHAYTTSS PRSEPTDDKW WLKGRTLFSE ITNGLGTGCH NAFDTHSPSY GIKFTNCRAV GDFRGVDTGG AGFQIRGDRS SLVDCTAINS KIGAAFTAVN ISGNSELYIS GFTYEGPAGH LALSLSGKAG QVNRVTISDS RWKTLEQYAT AITNVEVSAS NVEAVVDSAT TASAAWRIGE GATLRTRGGA ARFSAGSGHS VISLAASGAK VDVGDLEVTG SSFMQYLLAT LSQYAGDVYI EADLDGAIPG NPVGGGGTDL KAAVVYTAGN KFRRPLAYRA LTIGNANGNT LGLNYSGHDV ITWEITATVA GANVNGITPG AFIGQQLNIG SSPASTQQLI INNGTNIAMG HAVTLEAGRG VTLYWNGANW RSGSV //