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ESX secretion system protein YueB (Bacteriophage SPP1 adsorption protein YueB) (Bacteriophage SPP1 receptor protein YueB)

 YUEB_BACSU              Reviewed;        1076 AA.
O32101;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
26-FEB-2020, entry version 88.
RecName: Full=ESX secretion system protein YueB {ECO:0000305};
AltName: Full=Bacteriophage SPP1 adsorption protein YueB {ECO:0000305};
AltName: Full=Bacteriophage SPP1 receptor protein YueB {ECO:0000305};
Name=yueB; OrderedLocusNames=BSU31860;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[2]
FUNCTION AS A RECEPTOR FOR SPP1.
PubMed=15576783; DOI=10.1128/jb.186.24.8337-8346.2004;
Sao-Jose C., Baptista C., Santos M.A.;
"Bacillus subtilis operon encoding a membrane receptor for bacteriophage
SPP1.";
J. Bacteriol. 186:8337-8346(2004).
[3]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=168, and ATCC 6051;
PubMed=23861817; DOI=10.1371/journal.pone.0067840;
Baptista C., Barreto H.C., Sao-Jose C.;
"High levels of DegU-P activate an Esat-6-like secretion system in Bacillus
subtilis.";
PLoS ONE 8:E67840-E67840(2013).
[4]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=168 / PY79;
PubMed=24798022; DOI=10.1371/journal.pone.0096267;
Huppert L.A., Ramsdell T.L., Chase M.R., Sarracino D.A., Fortune S.M.,
Burton B.M.;
"The ESX system in Bacillus subtilis mediates protein secretion.";
PLoS ONE 9:E96267-E96267(2014).
-!- FUNCTION: Required for YukE secretion. Probable component or regulator
of the ESX/ESAT-6-like secretion system (BsEss) (PubMed:23861817,
PubMed:24798022). Bacteriophage SPP1 receptor. Essential for the
irreversible adsorption of the bacteriophage (PubMed:15576783).
{ECO:0000269|PubMed:15576783, ECO:0000269|PubMed:23861817,
ECO:0000269|PubMed:24798022}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000255}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are blocked in YukE
secretion. {ECO:0000269|PubMed:23861817, ECO:0000269|PubMed:24798022}.
-!- SIMILARITY: Belongs to the EsaA family. {ECO:0000305}.
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EMBL; AL009126; CAB15174.1; -; Genomic_DNA.
PIR; C70007; C70007.
RefSeq; NP_391064.1; NC_000964.3.
RefSeq; WP_003244105.1; NZ_JNCM01000033.1.
SMR; O32101; -.
IntAct; O32101; 22.
STRING; 224308.BSU31860; -.
PaxDb; O32101; -.
PRIDE; O32101; -.
EnsemblBacteria; CAB15174; CAB15174; BSU31860.
GeneID; 936567; -.
KEGG; bsu:BSU31860; -.
PATRIC; fig|224308.179.peg.3452; -.
eggNOG; COG1511; LUCA.
OMA; MYNFYKP; -.
BioCyc; BSUB:BSU31860-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
InterPro; IPR023838; T7SS_EsaA.
TIGRFAMs; TIGR03929; T7_esaA_Nterm; 1.
1: Evidence at protein level;
Cell membrane; Coiled coil; Membrane; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1..1076
/note="ESX secretion system protein YueB"
/id="PRO_0000066542"
TRANSMEM 9..29
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 904..924
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 938..958
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 964..984
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 995..1015
/note="Helical"
/evidence="ECO:0000255"
TRANSMEM 1040..1060
/note="Helical"
/evidence="ECO:0000255"
COILED 552..622
/evidence="ECO:0000255"
SEQUENCE 1076 AA; 119982 MW; CC1A368DF673A53C CRC64;
MTEQRKSLIK LISAVIIILL LPVLFFRFIG DDPTKKAVNS TRQIAVVNED TGVLSDEVKS
DEEDKSAQFG KEVAAVLGER PDYSWTVVNR SAAETGLASK KYDAIVYIPS DFSKNILSYD
KDHPQKATLE FSIQDNLNAV NKEKVQRELE DAQKTMNKKM SALYWNFVSQ KVDNIRGEFD
KIVNKESEFQ NVMYNFYKPS SNDLAGEIKQ QKDLIDELKK SMNEAQGTTK EKASTAEEAK
NTLKEFIDTV ERYKEYQENQ KKLLLAAQDS TQQQIRTGLD AIQAQQKANQ FSERMSGLAT
GIGQAKTQIG LTNLALNNAE KLRQNQVPLQ EMGMKKIEND MFNAFLSRYK SQYEAIKYQN
LNQLQENIGK NRLSLLKPKE SDEKEDGEDT SDNKDDTDKE DIEDIKLDLE KQRDELKNVA
TEIKDISEGL KEPEQEKPTT PDAEEPSTDD SPNTEEPSND IPTSDDQPTN EDTGSSEEGT
QDNGSQNDVQ TNIETGQKHQ ESSKNVPEQD TNTENTGTSK TDFSLIELAD ENDGSNQSDG
LQGDGADGET DISGAKKRLN EAAIKLEEIE NALQEKQEEH NNKLEKHIDE LNQEIKELNK
TVSKLNDQIG DLTKKLVDFD NNVNDAYRLI YNLEDEIIQT LQSRGYIDQK EKLSSIFSSR
IETDNISNLM KYYNSLNLYK STLNDNLDLG SLTIIKGEVI QEQDGNVQSV LALTPEESAS
WEALKNNTMQ TDEDINSFID GMTKFADDYS GYIRDSQAGV LDELTKISES AAKASEQLVT
GATQESATFS NDGLSGTMAL SVQDTVGQEV LQMSDMMGSL SDRQSGIIDY TTNMQQSVND
VQAKADTLNN NWGKNVASTK LVRNDVYGIL GNTLVDGQNN GYVYDYLANP LKISGEVPEE
KIQTVPPVVI LVIVLISSLL IGYFSSYYQN APLLVKGALF GILNILVGLM ISLFGLNIYS
LPDDQTIKWS VFTILLLVAS SAFIRTAFRF GSIPGWVASA AMILFYVAPL IDLIMPNFTF
EDPVSKVYID IQYGTGHLFT MGITVLLIIT VIAVALPLII RLMAEHTAES DETYEA


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WP1678: Nucleotide excision repair
WP2218: sGC
WP1690: Propanoate metabolism
WP1165: G Protein Signaling Pathways
WP1625: Base excision repair
WP813: G Protein Signaling Pathways
WP1694: Pyrimidine metabolism
WP232: G Protein Signaling Pathways
WP731: Sterol regulatory element binding protein related
WP1654: gamma-Hexachlorocyclohexane degradation
WP1661: Glyoxylate and dicarboxylate metabolism
WP210: Cytoplasmic Ribosomal Proteins
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WP1438: Influenza A virus infection
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Related Genes :
[yueB BSU31860] ESX secretion system protein YueB (Bacteriophage SPP1 adsorption protein YueB) (Bacteriophage SPP1 receptor protein YueB)
[SPP1 BNSP OPN PSEC0156] Osteopontin (Bone sialoprotein 1) (Nephropontin) (Secreted phosphoprotein 1) (SPP-1) (Urinary stone protein) (Uropontin)
[SGPP1 SPP1] Sphingosine-1-phosphate phosphatase 1 (SPPase1) (Spp1) (hSPP1) (hSPPase1) (EC 3.1.3.-) (Sphingosine-1-phosphatase 1) (Sphingosine-1-phosphate phosphohydrolase 1) (SPP-1)
[Sgpp1 Spp1 Spph1] Sphingosine-1-phosphate phosphatase 1 (SPP) (SPPase1) (mSPP1) (EC 3.1.3.-) (Sphingosine-1-phosphatase 1)
[Sgpp1] Sphingosine-1-phosphate phosphatase 1 (SPPase1) (Spp1) (EC 3.1.3.-) (Sphingosine-1-phosphatase 1)
[1] Terminase small subunit (G1P) (Terminase, small subunit gp1)
[12] Pre-neck appendage protein (Gene product 12) (gp12) (NP1) (Protein p12) [Cleaved into: gp12*]
[eccCb1 snm2 Rv3871] ESX-1 secretion system protein EccCb1 (ESX conserved component Cb1) (Snm2 secretory protein) (Type VII secretion system protein EccCb1) (T7SS protein EccCb1)
[eccB1 Rv3869] ESX-1 secretion system ATPase EccB1 (EC 3.6.-.-) (ESX conserved component B1) (Type VII secretion system protein EccB1) (T7SS protein EccB1)
[botD] Botulinum neurotoxin type D (BoNT/D) (Bontoxilysin-D) [Cleaved into: Botulinum neurotoxin D light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin D heavy chain (HC)]
[] Botulinum neurotoxin type C (BoNT/C) (Bontoxilysin-C1) (BoNT/C1) (Botulinum neurotoxin type C1) [Cleaved into: Botulinum neurotoxin C light chain (LC) (EC 3.4.24.69); Botulinum neurotoxin C heavy chain (HC)]
[] Endonuclease V (EC 3.2.2.17) (DNA-(apurinic or apyrimidinic site) lyase) (AP lyase) (EC 4.2.99.18) (T4 pyrimidine dimer glycosylase) (T4-Pdg)
[] Tail spike protein (TSP) (Endo-N-acetylneuraminidase) (Endo-N) (EC 3.2.1.129) (Endo-alpha-sialidase) (EndoNF) (G102) [Cleaved into: C-terminal chaperone protein]
[doc] Protein kinase doc (EC 2.7.11.1) (Death on curing protein) (Toxin doc)
[yukB yukA yukBA BSU31875 BSU31880] ESX secretion system protein YukB
[rpsA ssyF b0911 JW0894] 30S ribosomal protein S1 (Bacteriophage Q beta RNA-directed RNA polymerase subunit I) (Small ribosomal subunit protein bS1)
[A lambdap02] Terminase, large subunit (DNA-packaging protein A) (Large terminase protein) (gpA) [Includes: Endonuclease (EC 3.1.21.4); Helicase (EC 3.6.4.12); ATPase (EC 3.6.4.-)]
[5] Major capsid protein (Gene product 5) (gp5) (Major head protein)
[2] DNA polymerase (EC 2.7.7.7) (EC 3.1.11.-) (Gene product 2) (gp2) (Protein p2)
[1] DNA replication protein 1 (Gene product 1) (gp1)
[VII] Transglycosylase (EC 4.2.2.n1) (Protein P7)
[17 lysa lyz] SAR-endolysin (EC 3.2.1.17) (Endolysin) (Gene product 17) (gp17) (Lysis protein) (Lysozyme) (Muramidase)
[CD44 LHR MDU2 MDU3 MIC4] CD44 antigen (CDw44) (Epican) (Extracellular matrix receptor III) (ECMR-III) (GP90 lymphocyte homing/adhesion receptor) (HUTCH-I) (Heparan sulfate proteoglycan) (Hermes antigen) (Hyaluronate receptor) (Phagocytic glycoprotein 1) (PGP-1) (Phagocytic glycoprotein I) (PGP-I) (CD antigen CD44)
[16] Peptidoglycan transglycosylase gp16 (EC 4.2.2.n1) (Internal core protein gp16)
[tufA b3339 JW3301] Elongation factor Tu 1 (EF-Tu 1) (Bacteriophage Q beta RNA-directed RNA polymerase subunit III) (P-43)
[A Mup03] DDE-recombinase A (EC 3.1.22.-) (EC 6.5.1.-) (DDE-transposase A) (Gene product 03) (gp03) (Gene product A) (gpA) (MuA)
[C; NU3 lambdap05] Capsid assembly protease C (EC 3.4.21.-) (Gene product C) (GPC) (Minor capsid protein C)
[Y10A 24.1] RNA ligase 2 (EC 6.5.1.3) (Rnl2)
[tufB b3980 JW3943] Elongation factor Tu 2 (EF-Tu 2) (Bacteriophage Q beta RNA-directed RNA polymerase subunit III) (P-43)
[FAM20C DMP4] Extracellular serine/threonine protein kinase FAM20C (EC 2.7.11.1) (Dentin matrix protein 4) (DMP-4) (Golgi casein kinase) (Golgi-enriched fraction casein kinase) (GEF-CK)

Bibliography :