ID   TIPJ_LAMBD              Reviewed;        1132 AA.
AC   P03749;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   29-SEP-2021, entry version 105.
DE   RecName: Full=Tip attachment protein J;
DE   AltName: Full=Central tail fiber;
DE   AltName: Full=Host specificity protein J;
GN   Name=J; OrderedLocusNames=lambdap21;
OS   Escherichia phage lambda (Bacteriophage lambda).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Lambdavirus.
OX   NCBI_TaxID=10710;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA   Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT   "Nucleotide sequence of bacteriophage lambda DNA.";
RL   J. Mol. Biol. 162:729-773(1982).
RN   [2]
RP   FUNCTION.
RX   PubMed=6228546; DOI=10.1128/jb.157.1.165-170.1984;
RA   Roessner C.A., Ihler G.M.;
RT   "Proteinase sensitivity of bacteriophage lambda tail proteins gpJ and pH in
RT   complexes with the lambda receptor.";
RL   J. Bacteriol. 157:165-170(1984).
RN   [3]
RP   INTERACTION WITH HOST LAMB.
RX   PubMed=8106335; DOI=10.1128/jb.176.4.941-947.1994;
RA   Werts C., Michel V., Hofnung M., Charbit A.;
RT   "Adsorption of bacteriophage lambda on the LamB protein of Escherichia coli
RT   K-12: point mutations in gene J of lambda responsible for extended host
RT   range.";
RL   J. Bacteriol. 176:941-947(1994).
RN   [4]
RP   INTERACTION WITH HOST LAMB.
RX   PubMed=9826917; DOI=10.1016/s0923-2508(99)80009-6;
RA   Wang J., Michel V., Hofnung M., Charbit A.;
RT   "Cloning of the J gene of bacteriophage lambda, expression and
RT   solubilization of the J protein: first in vitro studies on the interactions
RT   between J and LamB, its cell surface receptor.";
RL   Res. Microbiol. 149:611-624(1998).
RN   [5]
RP   INTERACTION WITH HOST LAMB.
RX   PubMed=10629200; DOI=10.1128/jb.182.2.508-512.2000;
RA   Wang J., Hofnung M., Charbit A.;
RT   "The C-terminal portion of the tail fiber protein of bacteriophage lambda
RT   is responsible for binding to LamB, its receptor at the surface of
RT   Escherichia coli K-12.";
RL   J. Bacteriol. 182:508-512(2000).
RN   [6]
RP   INTERACTION WITH HOST LAMB.
RX   PubMed=16489764; DOI=10.1021/bi051800v;
RA   Berkane E., Orlik F., Stegmeier J.F., Charbit A., Winterhalter M., Benz R.;
RT   "Interaction of bacteriophage lambda with its cell surface receptor: an in
RT   vitro study of binding of the viral tail protein gpJ to LamB
RT   (Maltoporin).";
RL   Biochemistry 45:2708-2720(2006).
RN   [7]
RP   REVIEW.
RX   PubMed=23202520; DOI=10.3390/v4113162;
RA   Chatterjee S., Rothenberg E.;
RT   "Interaction of bacteriophage l with its E. coli receptor, LamB.";
RL   Viruses 4:3162-3178(2012).
CC   -!- FUNCTION: Attaches the virion to the host receptor LamB, inducing viral
CC       DNA ejection. During tail assembly, initiates distal tail tip assembly
CC       by interacting with gpI, gpL and gpK. During virus entry to host cell,
CC       binds strongly to host LamB in an irreversible attachment. The binding
CC       induces structural changes in the tail leading to viral DNA injection
CC       through LamB trimeric pore. {ECO:0000269|PubMed:6228546}.
CC   -!- SUBUNIT: Interacts with host LamB. {ECO:0000269|PubMed:10629200,
CC       ECO:0000269|PubMed:16489764, ECO:0000269|PubMed:8106335,
CC       ECO:0000269|PubMed:9826917}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}. Host cytoplasm
CC       {ECO:0000305}.
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DR   EMBL; J02459; AAA96553.1; -; Genomic_DNA.
DR   PIR; D43009; QSBPL.
DR   RefSeq; NP_040600.1; NC_001416.1.
DR   GeneID; 2703516; -.
DR   KEGG; vg:2703516; -.
DR   Proteomes; UP000001711; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0098015; C:virus tail; IEA:UniProtKB-KW.
DR   GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0046813; P:receptor-mediated virion attachment to host cell; IMP:CACAO.
DR   GO; GO:0099001; P:viral genome ejection through host cell envelope, long flexible tail mechanism; IEA:UniProtKB-KW.
DR   GO; GO:0098003; P:viral tail assembly; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IDA:UniProtKB.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR015406; DUF1983.
DR   InterPro; IPR021034; DUF3672.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032876; J_dom.
DR   Pfam; PF09327; DUF1983; 1.
DR   Pfam; PF12421; DUF3672; 1.
DR   Pfam; PF13550; Phage-tail_3; 1.
DR   SMART; SM00060; FN3; 2.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   PROSITE; PS50853; FN3; 1.
PE   1: Evidence at protein level;
KW   Host cytoplasm; Host-virus interaction; Late protein; Reference proteome;
KW   Repeat; Viral attachment to host cell;
KW   Viral attachment to host entry receptor;
KW   Viral genome ejection through host cell envelope;
KW   Viral long flexible tail ejection system;
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..1132
FT                   /note="Tip attachment protein J"
FT                   /id="PRO_0000077645"
FT   DOMAIN          618..711
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          712..807
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   REGION          883..1132
FT                   /note="Interaction with host LamB"
FT                   /evidence="ECO:0000269|PubMed:10629200"
SQ   SEQUENCE   1132 AA;  124422 MW;  53D4AC9044CF3C05 CRC64;
     MGKGSSKGHT PREAKDNLKS TQLLSVIDAI SEGPIEGPVD GLKSVLLNST PVLDTEGNTN
     ISGVTVVFRA GEQEQTPPEG FESSGSETVL GTEVKYDTPI TRTITSANID RLRFTFGVQA
     LVETTSKGDR NPSEVRLLVQ IQRNGGWVTE KDITIKGKTT SQYLASVVMG NLPPRPFNIR
     MRRMTPDSTT DQLQNKTLWS SYTEIIDVKQ CYPNTALVGV QVDSEQFGSQ QVSRNYHLRG
     RILQVPSNYN PQTRQYSGIW DGTFKPAYSN NMAWCLWDML THPRYGMGKR LGAADVDKWA
     LYVIGQYCDQ SVPDGFGGTE PRITCNAYLT TQRKAWDVLS DFCSAMRCMP VWNGQTLTFV
     QDRPSDKTWT YNRSNVVMPD DGAPFRYSFS ALKDRHNAVE VNWIDPNNGW ETATELVEDT
     QAIARYGRNV TKMDAFGCTS RGQAHRAGLW LIKTELLETQ TVDFSVGAEG LRHVPGDVIE
     ICDDDYAGIS TGGRVLAVNS QTRTLTLDRE ITLPSSGTAL ISLVDGSGNP VSVEVQSVTD
     GVKVKVSRVP DGVAEYSVWE LKLPTLRQRL FRCVSIREND DGTYAITAVQ HVPEKEAIVD
     NGAHFDGEQS GTVNGVTPPA VQHLTAEVTA DSGEYQVLAR WDTPKVVKGV SFLLRLTVTA
     DDGSERLVST ARTTETTYRF TQLALGNYRL TVRAVNAWGQ QGDPASVSFR IAAPAAPSRI
     ELTPGYFQIT ATPHLAVYDP TVQFEFWFSE KQIADIRQVE TSTRYLGTAL YWIAASINIK
     PGHDYYFYIR SVNTVGKSAF VEAVGRASDD AEGYLDFFKG KITESHLGKE LLEKVELTED
     NASRLEEFSK EWKDASDKWN AMWAVKIEQT KDGKHYVAGI GLSMEDTEEG KLSQFLVAAN
     RIAFIDPANG NETPMFVAQG NQIFMNDVFL KRLTAPTITS GGNPPAFSLT PDGKLTAKNA
     DISGSVNANS GTLSNVTIAE NCTINGTLRA EKIVGDIVKA ASAAFPRQRE SSVDWPSGTR
     TVTVTDDHPF DRQIVVLPLT FRGSKRTVSG RTTYSMCYLK VLMNGAVIYD GAANEAVQVF
     SRIVDMPAGR GNVILTFTLT STRHSADIPP YTFASDVQVM VIKKQALGIS VV