BP44_BPMU
ID BP44_BPMU Reviewed; 379 AA.
AC P08558;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 23-FEB-2022, entry version 93.
DE RecName: Full=Baseplate hub protein gp44;
DE AltName: Full=43 kDa tail protein;
DE AltName: Full=Gene product 44;
DE Short=gp44;
DE AltName: Full=Gene product P;
DE Short=gpP;
GN Name=P; OrderedLocusNames=Mup44;
OS Escherichia phage Mu (Bacteriophage Mu).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Muvirus.
OX NCBI_TaxID=10677;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MUCTS62PAP1;
RX PubMed=2968539; DOI=10.1093/nar/16.11.5211;
RA Chaconas G., Gloor G.;
RT "Sequence of bacteriophage Mu N and P genes.";
RL Nucleic Acids Res. 16:5211-5212(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11922669; DOI=10.1006/jmbi.2002.5437;
RA Morgan G.J., Hatfull G.F., Casjens S., Hendrix R.W.;
RT "Bacteriophage Mu genome sequence: analysis and comparison with Mu-like
RT prophages in Haemophilus, Neisseria and Deinococcus.";
RL J. Mol. Biol. 317:337-359(2002).
RN [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=3904174; DOI=10.1016/0042-6822(85)90388-5;
RA Grundy F.J., Howe M.M.;
RT "Morphogenetic structures present in lysates of amber mutants of
RT bacteriophage Mu.";
RL Virology 143:485-504(1985).
RN [4]
RP INDUCTION.
RX PubMed=8293968; DOI=10.1093/genetics/135.3.619;
RA Chiang L.W., Howe M.M.;
RT "Mutational analysis of a C-dependent late promoter of bacteriophage Mu.";
RL Genetics 135:619-629(1993).
RN [5]
RP CHARACTERIZATION, SUBUNIT, AND CLEAVAGE OF C-TERMINUS.
RX PubMed=15944413; DOI=10.1093/jb/mvi076;
RA Kitazawa D., Takeda S., Kageyama Y., Tomihara M., Fukada H.;
RT "Expression and characterization of a baseplate protein for bacteriophage
RT Mu, gp44.";
RL J. Biochem. 137:601-606(2005).
RN [6]
RP REVIEW.
RX PubMed=22297511; DOI=10.1007/978-1-4614-0980-9_5;
RA Leiman P.G., Shneider M.M.;
RT "Contractile tail machines of bacteriophages.";
RL Adv. Exp. Med. Biol. 726:93-114(2012).
RN [7]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=27555589; DOI=10.1073/pnas.1607966113;
RA Buettner C.R., Wu Y., Maxwell K.L., Davidson A.R.;
RT "Baseplate assembly of phage Mu: Defining the conserved core components of
RT contractile-tailed phages and related bacterial systems.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:10174-10179(2016).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16125724; DOI=10.1016/j.jmb.2005.07.044;
RA Kondou Y., Kitazawa D., Takeda S., Tsuchiya Y., Yamashita E., Mizuguchi M.,
RA Kawano K., Tsukihara T.;
RT "Structure of the central hub of bacteriophage Mu baseplate determined by
RT X-ray crystallography of gp44.";
RL J. Mol. Biol. 352:976-985(2005).
CC -!- FUNCTION: Forms the central cylindrical hub of the baseplate and plays
CC an important role in baseplate and tail assembly (Probable). Core
CC component of the initiator complex that triggers the tail tube
CC polymerization during tail assembly (Probable). Forms a conduit that
CC probably functions as an extension of the tail tube allowing viral DNA
CC release during ejection. Might facilitate the interaction of the virus
CC with the host cell surface through electrostatic interactions during
CC virus entry into host cell. {ECO:0000305}.
CC -!- SUBUNIT: Heterotrimer of one uncleaved (42 kDa) and two cleaved (40
CC kDa) forms. Forms a hub-like structure with an inner diameter of 25
CC Angstroms through which DNA can presumably pass during infection. Part
CC of a complex composed of three DNA circularization protein N, three
CC baseplate hub protein gp44 and three sub-complex wedge (made of two
CC copies of each baseplate protein gp46, gp47 and gp48) that forms the
CC baseplate (PubMed:27555589). {ECO:0000269|PubMed:15944413,
CC ECO:0000269|PubMed:16125724, ECO:0000269|PubMed:27555589}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16125724,
CC ECO:0000269|PubMed:27555589}. Host cytoplasm
CC {ECO:0000305|PubMed:16125724}. Note=Baseplate protein.
CC {ECO:0000269|PubMed:27555589}.
CC -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC Expression of late genes is activated by the viral late transcription
CC activator C. {ECO:0000269|PubMed:8293968}.
CC -!- DOMAIN: C-terminal region forms a flexible domain. {ECO:0000305}.
CC -!- PTM: Cleavage of the C-terminus gives rise to a shorter 40 kDa form.
CC -!- DISRUPTION PHENOTYPE: No tail is synthesized.
CC {ECO:0000269|PubMed:3904174}.
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DR EMBL; X06796; CAA29956.1; -; Genomic_DNA.
DR EMBL; AF083977; AAF01122.1; -; Genomic_DNA.
DR PIR; S01891; ZPBPMU.
DR RefSeq; NP_050648.1; NC_000929.1.
DR PDB; 1WRU; X-ray; 2.10 A; A=1-379.
DR PDBsum; 1WRU; -.
DR SMR; P08558; -.
DR GeneID; 2636285; -.
DR KEGG; vg:2636285; -.
DR EvolutionaryTrace; P08558; -.
DR Proteomes; UP000002611; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098025; C:virus tail, baseplate; IEA:UniProtKB-KW.
DR GO; GO:0099000; P:viral genome ejection through host cell envelope, contractile tail mechanism; IEA:UniProtKB-KW.
DR GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1920.10; -; 1.
DR InterPro; IPR023399; Baseplate-like_2-layer_sand.
DR InterPro; IPR026276; Baseplate_GpP.
DR PIRSF; PIRSF004440; GpP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Host cytoplasm; Late protein; Reference proteome;
KW Viral baseplate protein; Viral contractile tail ejection system;
KW Viral genome ejection through host cell envelope;
KW Viral penetration into host cytoplasm; Viral release from host cell;
KW Viral tail assembly; Viral tail protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..379
FT /note="Baseplate hub protein gp44"
FT /id="PRO_0000077692"
FT DNA_BIND 209..228
FT /note="H-T-H motif"
FT /evidence="ECO:0000255"
FT REGION 344..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 61..75
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 91..95
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 149..158
FT /evidence="ECO:0007829|PDB:1WRU"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:1WRU"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 256..274
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 275..285
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 297..302
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 312..322
FT /evidence="ECO:0007829|PDB:1WRU"
FT TURN 323..325
FT /evidence="ECO:0007829|PDB:1WRU"
FT STRAND 326..335
FT /evidence="ECO:0007829|PDB:1WRU"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1WRU"
SQ SEQUENCE 379 AA; 41785 MW; E09AED2158D13CA1 CRC64;
MSNTVTLRAD GRLFTGWTSV SVTRSIESVA GYFELGVNVP PGTDLSGLAP GKKFTLEIGG
QIVCTGYIDS RRRQMTADSM KITVAGRDKT ADLIDCAAVY SGGQWKNRTL EQIARDLCAP
YGVTVRWELS DKESSAAFPG FTLDHSETVY EALVRASRAR GVLMTSNAAG ELVFSRAAST
ATDELVLGEN LLTLDFEEDF RDRFSEYTVK GYARANGAEG DDIDAKSIVS RKGTATDSDV
TRYRPMIIIA DSKITAKDAQ ARALREQRRR LAKSITFEAE IDGWTRKDGQ LWMPNLLVTI
DASKYAIKTT ELLVSKVTLI LNDQDGLKTR VSLAPREGFL VPVESDRKNR KGGDSNGGID
ALVEDYYRRH PEKTPPWKE
