YUKC_BACSU
ID YUKC_BACSU Reviewed; 451 AA.
AC P71070; Q795L4;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=ESX secretion system protein YukC {ECO:0000305};
GN Name=yukC; OrderedLocusNames=BSU31890;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9168598; DOI=10.1099/00221287-143-5-1489;
RA Oudega B., Vandenbol M., Koningstein G.;
RT "A 12kb nucleotide sequence containing the alanine dehydrogenase gene at
RT 279 degree on the Bacillus subtilis chromosome.";
RL Microbiology 143:1489-1491(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=15576783; DOI=10.1128/jb.186.24.8337-8346.2004;
RA Sao-Jose C., Baptista C., Santos M.A.;
RT "Bacillus subtilis operon encoding a membrane receptor for bacteriophage
RT SPP1.";
RL J. Bacteriol. 186:8337-8346(2004).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168, and ATCC 6051;
RX PubMed=23861817; DOI=10.1371/journal.pone.0067840;
RA Baptista C., Barreto H.C., Sao-Jose C.;
RT "High levels of DegU-P activate an Esat-6-like secretion system in Bacillus
RT subtilis.";
RL PLoS ONE 8:E67840-E67840(2013).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=24798022; DOI=10.1371/journal.pone.0096267;
RA Huppert L.A., Ramsdell T.L., Chase M.R., Sarracino D.A., Fortune S.M.,
RA Burton B.M.;
RT "The ESX system in Bacillus subtilis mediates protein secretion.";
RL PLoS ONE 9:E96267-E96267(2014).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=34280190; DOI=10.1371/journal.pgen.1009682;
RA Kobayashi K.;
RT "Diverse LXG toxin and antitoxin systems specifically mediate intraspecies
RT competition in Bacillus subtilis biofilms.";
RL PLoS Genet. 17:e1009682-e1009682(2021).
RN [7] {ECO:0007744|PDB:6Z0F}
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 1-413.
RA Tassinari M., Doan T., Bellinzoni M., Chabalier M., Ben-Assaya M.,
RA Martinez M., Gaday Q., Alzari P.M., Cascales E., Fronzes R., Gubellini F.;
RT "Central role and structure of the membrane pseudokinase YukC in the
RT antibacterial Bacillus subtilis Type VIIb Secretion System.";
RL Submitted (MAY-2020) to the PDB data bank.
CC -!- FUNCTION: Required for YukE secretion. Probable component or regulator
CC of the ESX/ESAT-6-like secretion system (BsEss) (PubMed:23861817,
CC PubMed:24798022). Required to deliver LXG toxins to target cells
CC (PubMed:34280190). {ECO:0000269|PubMed:23861817,
CC ECO:0000269|PubMed:24798022, ECO:0000269|PubMed:34280190}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are blocked in YukE
CC secretion (PubMed:23861817, PubMed:24798022). They display an increased
CC bacteriophage SPP1 resistance phenotype (PubMed:15576783). Loss of
CC delivery of LXG toxins to target cells (PubMed:34280190).
CC {ECO:0000269|PubMed:15576783, ECO:0000269|PubMed:23861817,
CC ECO:0000269|PubMed:24798022, ECO:0000269|PubMed:34280190}.
CC -!- SIMILARITY: Belongs to the EssB family. {ECO:0000305}.
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DR EMBL; Z82015; CAB04771.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15177.1; -; Genomic_DNA.
DR PIR; E70013; E70013.
DR RefSeq; NP_391067.1; NC_000964.3.
DR RefSeq; WP_003243575.1; NZ_JNCM01000033.1.
DR PDB; 6Z0F; X-ray; 2.55 A; A/B=1-413.
DR PDBsum; 6Z0F; -.
DR AlphaFoldDB; P71070; -.
DR SMR; P71070; -.
DR IntAct; P71070; 1.
DR STRING; 224308.BSU31890; -.
DR PaxDb; P71070; -.
DR EnsemblBacteria; CAB15177; CAB15177; BSU_31890.
DR GeneID; 936572; -.
DR KEGG; bsu:BSU31890; -.
DR PATRIC; fig|224308.179.peg.3454; -.
DR eggNOG; COG4499; Bacteria.
DR OMA; FLHYGVK; -.
DR PhylomeDB; P71070; -.
DR BioCyc; BSUB:BSU31890-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.680; -; 1.
DR InterPro; IPR018778; T7SS_EssB.
DR InterPro; IPR042565; T7SS_EssB_C.
DR Pfam; PF10140; YukC; 1.
DR TIGRFAMs; TIGR03926; T7_EssB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coiled coil; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..451
FT /note="ESX secretion system protein YukC"
FT /id="PRO_0000383634"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 376..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 362..447
FT /evidence="ECO:0000255"
FT COMPBIAS 402..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 8..13
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 37..41
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 83..98
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:6Z0F"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 140..155
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 161..165
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 175..181
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 186..205
FT /evidence="ECO:0007829|PDB:6Z0F"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 212..241
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 243..258
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:6Z0F"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 279..293
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 328..337
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 341..357
FT /evidence="ECO:0007829|PDB:6Z0F"
FT HELIX 363..383
FT /evidence="ECO:0007829|PDB:6Z0F"
SQ SEQUENCE 451 AA; 52161 MW; 9F3FFB757377BA2D CRC64;
MSGEQKSYLE NQLEAVAEKT DAGYTFTFQR EKIKLLDGLE ANVIKDINPF FHKEIDVTDD
EVIITIQPPS SYKAFRFMKA KDKKSKWQFA YQLVQAVQQH NLSRLNLIVA PENIVFDKGL
TPYFLHYGVK ESIPPYERDE ERVWQELKAA AALAVDGAFA FEDYLKFNET LTFSAEAKAI
LDAESYDDLL ELIQTHIDEL EAKAKTYIHI PRKKWNIQRY IGLGLIVLLV PALIYSMYAL
FFAQPKHQAI VDSNRAFLNK QYSEVISTLS KYDAESLPES VQYQLATSYV EVENLGSAKT
KNIENNLVTL QSDPQHFLYW IDYGRGEYKE AISIGRKLEY NDYIYFALAK YKQQLLSEDT
NDEDIQKELD SVNSELEKAQ KERQENKQSN SETSLVDTSE EQTQTDEEKQ AEEKAAEEKA
AAEEKAKKEE QKEKEDEKKE TEKKDEKKDD K
