TMP_BPSPB
ID TMP_BPSPB Reviewed; 2285 AA.
AC O64046;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 29-SEP-2021, entry version 91.
DE RecName: Full=Probable tape measure protein {ECO:0000250|UniProtKB:O64314};
DE Short=TMP;
DE AltName: Full=Transglycosylase {ECO:0000250|UniProtKB:P27380};
DE EC=4.2.2.n1 {ECO:0000250|UniProtKB:P27380};
GN Name=yomI {ECO:0000312|EMBL:AAC13005.1};
OS Bacillus phage SPbeta (Bacillus phage SPBc2) (Bacteriophage SP-beta).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Spbetavirus.
OX NCBI_TaxID=66797 {ECO:0000312|Proteomes:UP000009091};
OH NCBI_TaxID=1408; Bacillus pumilus (Bacillus mesentericus).
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1] {ECO:0000312|Proteomes:UP000009091}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9465078; DOI=10.1073/pnas.95.4.1692;
RA Lazarevic V., Soldo B., Duesterhoeft A., Hilbert H., Maueel C.,
RA Karamata D.;
RT "Introns and intein coding sequence in the ribonucleotide reductase genes
RT of Bacillus subtilis temperate bacteriophage SPbeta.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1692-1697(1998).
RN [2]
RP FUNCTION.
RX PubMed=14763988; DOI=10.1046/j.1365-2958.2003.03894.x;
RA Moak M., Molineux I.J.;
RT "Peptidoglycan hydrolytic activities associated with bacteriophage
RT virions.";
RL Mol. Microbiol. 51:1169-1183(2004).
CC -!- FUNCTION: Serves as a base for tail tube protein polymerization and
CC acts as a template for tail length determination. Exolysin involved in
CC host peptidoglycan digestion necessary for viral DNA entry into the
CC host cell (PubMed:14763988). {ECO:0000250|UniProtKB:O64314,
CC ECO:0000269|PubMed:14763988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC non-reducing ends of the peptidoglycan chains, with concomitant
CC formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC Evidence={ECO:0000250|UniProtKB:P27380};
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the P2likevirus tape measure protein family.
CC {ECO:0000305}.
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DR EMBL; AF020713; AAC13005.1; -; Genomic_DNA.
DR PIR; T12796; T12796.
DR RefSeq; NP_046584.1; NC_001884.1.
DR SMR; O64046; -.
DR MEROPS; M23.A04; -.
DR PRIDE; O64046; -.
DR GeneID; 1261425; -.
DR KEGG; vg:1261425; -.
DR Proteomes; UP000009091; Genome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0098932; P:disruption by virus of host cell wall peptidoglycan during virus entry; IEA:UniProtKB-KW.
DR GO; GO:0044409; P:entry into host; IDA:UniProtKB.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
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 Gene3D; 2.70.70.10; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR016047; Peptidase_M23.
DR InterPro; IPR010090; Phage_tape_meas.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR Pfam; PF10145; PhageMin_Tail; 1.
DR Pfam; PF01464; SLT; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR SUPFAM; SSF53955; SSF53955; 1.
DR TIGRFAMs; TIGR01760; tape_meas_TP901; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Antimicrobial; Bacteriolytic enzyme; Coiled coil;
KW Degradation of host cell envelope components during virus entry;
KW Degradation of host peptidoglycans during virus entry; Lyase;
KW Reference proteome; 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; Virion; Virus entry into host cell.
FT CHAIN 1..2285
FT /note="Probable tape measure protein"
FT /evidence="ECO:0000250|UniProtKB:O64314"
FT /id="PRO_0000431948"
FT REGION 138..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..133
FT /evidence="ECO:0000255"
FT COILED 174..260
FT /evidence="ECO:0000255"
FT COILED 298..324
FT /evidence="ECO:0000255"
FT COILED 620..643
FT /evidence="ECO:0000255"
FT COILED 768..788
FT /evidence="ECO:0000255"
FT COILED 843..903
FT /evidence="ECO:0000255"
FT COILED 985..1030
FT /evidence="ECO:0000255"
FT COILED 1067..1089
FT /evidence="ECO:0000255"
FT COILED 1219..1262
FT /evidence="ECO:0000255"
FT COILED 1328..1394
FT /evidence="ECO:0000255"
FT COILED 1702..1729
FT /evidence="ECO:0000255"
FT COILED 1790..1837
FT /evidence="ECO:0000255"
FT COILED 1875..1930
FT /evidence="ECO:0000255"
FT COILED 1963..2074
FT /evidence="ECO:0000255"
FT COMPBIAS 164..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10071"
SQ SEQUENCE 2285 AA; 252312 MW; FF602C227754B357 CRC64;
MSQNLKIILT PQADTSSKTV EQLNQQIKSL EKKLNSLKLN TNIDSTTLKA LQEFSSAIDT
YQKNLKSYNQ TVKETSTVIK NADGSVEKLT QQYKKNGEIL QRETKIINNR NTALKQETQE
VNKLTQATEK LGQVQKKTVQ RNLQGQPTKV VQKNRHGFDD IVYTTDPKTN STSSKTTTNY
DQQRRAIEQL KQDLEKLRQQ GIVTDTTISS LGRKINTAQS AQQIEALQNR IRMLDDKSAA
VAKNNELKKT IELYQRQAQV NVQNLNTRYG SSMGSSNRQA VQDYLNAVNS LNVSTGSNNI
RSQIQSLNMQ FRELASNAQT AANQASSFGA ELTQTFKSMS TYLISGSLFY GAISGLKEMV
SQAIEIDTLM TNIRRVMNEP DYKYNELLQE SIDLGDTLSN KITDILQMTG DFGRMGFDES
ELSTLTKTAQ VLQNVSDLTP DDTVNTLTAA MLNFNIAAND SISIADKLNE VDNNYAVTTL
DLANSIRKAG STASTFGVEL NDLIGYTTAI ASTTRESGNI VGNSLKTIFA RIGNNQSSIK
ALEQIGISVK TAGGEAKSAS DLISEVAGKW DTLSDAQKQN TSIGVAGIYQ LSRFNAMMNN
FSIAQNAAKT AANSTGSAWS EQQKYADSLQ ARVNKLQNNF TEFAIAASDA FISDGLIEFT
QAAGSLLNAS TGVIKSVGFL PPLLAAVSTA TLLLSKNTRT LASSLILGTR AMGQETLATA
GLEAGMTRAA VASRVLKTAL RGLLVSTLVG GAFAALGWAL ESLISSFAEA KKAKDDFEQS
QQTNVEAITT NKDSTDKLIQ QYKELQKVKE SRSLTSDEEQ EYLQVTQQLA QTFPALVKGY
DSQGNAILKT NKELEKAIEN TKEYLALKKQ ETRDSAKKTF EDASKEIKKS KDELKQYKQI
ADYNDKGRPK WDLIADDDDY KVAADKAKQS MLKAQSDIES GNAKVKDSVL SIANAYSSID
ISNTLKTSIS DVVNKLNLKD DLDPEELEKF SSSLGKLQEK MQKALDSGDE KAFDNAKKDL
QSLLETYSKS DSSIDVFKMS FDKAQKNIKD GDKSLSSVKS EVGDLGETLA EAGNEAEDFG
KKLKEALDAN SVDDIKAAIK EMSDAMQFDS VQDVLNGDIF NNTKDQVAPL NDLLEKMAEG
KSISANEANT LIQKDKELAQ AISIENGVVK INRDEVIKQR KVKLDAYNDM VTYSNKLMKT
EVNNAIKTLN ADTLRIDSLK KLRKERKLDM SEAELSDLEV KSINNVADAK KELKKLEEKM
LQPGGYSNSQ IEAMQSVKSA LESYISASEE ATSTQEMNKQ ALVEAGTSLE NWTDQQEKAN
EETKTSMYVV DKYKEALEKV NAEIDKYNKQ VNDYPKYSQK YRDAIKKEIK ALQQKKKLMQ
EQAKLLKDQI KSGNITQYGI VTSTTSSGGT PSSTGGSYSG KYSSYINSAA SKYNVDPALI
AAVIQQESGF NAKARSGVGA MGLMQLMPAT AKSLGVNNAY DPYQNVMGGT KYLAQQLEKF
GGNVEKALAA YNAGPGNVIK YGGIPPFKET QNYVKKIMAN YSKSLSSATS SIASYYTNNS
AFRVSSKYGQ QESGLRSSPH KGTDFAAKAG TAIKSLQSGK VQIAGYSKTA GNWVVIKQDD
GTVAKYMHML NTPSVKAGQS VKAGQTIGKV GSTGNSTGNH LHLQIEQNGK TIDPEKYMQG
IGTSISDASQ AEAERQQGIA QAKSDLLSLQ GDISSVNDQI QELQYELVQS KLDEFDKRIG
DFDVRIAKDE SMANRYTSDS KEFRKYTSDQ KKAVAEQAKI QQQKVNWIQK EIKTNKALNS
AQRAQLQEEL KQAKLDLISV QDQVRELQKQ LVQSKVDETL KSIEKSSSKT QGKIKDVDNK
ISMTEEDEDK VKYYSKQIKL IQQQQKEAKK YIKQLEEQKK AAKGFPDIQE QITEEMQNWK
DKQKDFNLEL YNTKKSIKDI YKSLADEVVS IYKEMYEKMR DIELEAHQKA TQDLIDEIDK
TDDEAKFQKE LKERQDSIQK LTDQINQYSL DDSEFGKSKV KELTEQLQKE QLDLDDFLKD
RESNKRKEAL QDQLEKDEES INNKYDNLVN DERAFKKLED KIMNGKITDI AKQLNEFSKF
INTNMESIGK SISNNLIDKL KEASNALNTA VKGNTTGKKV SSFASGGYTG TGLGAGKLAF
LHDKELILNK TDTANILDTV KAVRETAVDD SPKWGQGVKL ADLIKKGITS IPSLVPNVNQ
SMLTNSLIPN LKKIEIPSKT IASSGDKTIN LTNTFHIDKL IGGESGARSM FESIKNEVVK
LNGSM
