YVGJ_BACSU
ID YVGJ_BACSU Reviewed; 617 AA.
AC O32206; Q7B2K8;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lipoteichoic acid synthase-like YvgJ;
DE Contains:
DE RecName: Full=Uncharacterized protein YvgJ;
DE Contains:
DE RecName: Full=Processed uncharacterized protein YvgJ;
GN Name=yvgJ; OrderedLocusNames=BSU33360;
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=9639930; DOI=10.1099/00221287-144-6-1593;
RA Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R.;
RT "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis
RT chromosome containing genes involved in metal ion uptake and a putative
RT sigma factor.";
RL Microbiology 144:1593-1600(1998).
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 NON-INVOLVEMENT IN LTA BIOSYNTHESIS.
RC STRAIN=168;
RX PubMed=17483484; DOI=10.1073/pnas.0701821104;
RA Gruendling A., Schneewind O.;
RT "Synthesis of glycerol phosphate lipoteichoic acid in Staphylococcus
RT aureus.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:8478-8483(2007).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Processed uncharacterized protein YvgJ]:
CC Secreted {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved. {ECO:0000250}.
CC -!- MISCELLANEOUS: Although its sequence similarity with the glycerol
CC phosphate lipoteichoic acid synthase LtaS, it cannot restore
CC staphylococcal growth and LTA synthesis after ltaS depletion.
CC -!- SIMILARITY: Belongs to the LTA synthase family. {ECO:0000305}.
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DR EMBL; AJ223978; CAA11716.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15341.1; -; Genomic_DNA.
DR PIR; G70039; G70039.
DR RefSeq; NP_391216.1; NC_000964.3.
DR RefSeq; WP_003243932.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32206; -.
DR SMR; O32206; -.
DR IntAct; O32206; 1.
DR STRING; 224308.BSU33360; -.
DR PaxDb; O32206; -.
DR PRIDE; O32206; -.
DR EnsemblBacteria; CAB15341; CAB15341; BSU_33360.
DR GeneID; 936006; -.
DR KEGG; bsu:BSU33360; -.
DR PATRIC; fig|224308.179.peg.3621; -.
DR eggNOG; COG1368; Bacteria.
DR InParanoid; O32206; -.
DR OMA; ADIWYYR; -.
DR PhylomeDB; O32206; -.
DR BioCyc; BSUB:BSU33360-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:InterPro.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR012160; LtaS-like.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR PIRSF; PIRSF005091; Mmb_sulf_HI1246; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
PE 3: Inferred from homology;
KW Cell membrane; Manganese; Membrane; Metal-binding; Reference proteome;
KW Secreted; Transmembrane; Transmembrane helix.
FT CHAIN 1..213
FT /note="Uncharacterized protein YvgJ"
FT /id="PRO_0000305377"
FT CHAIN 214..617
FT /note="Processed uncharacterized protein YvgJ"
FT /id="PRO_0000305378"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..41
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..617
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT ACT_SITE 293
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 293
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 408
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 467
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 468
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 213..214
FT /note="Cleavage"
FT /evidence="ECO:0000250"
SQ SEQUENCE 617 AA; 70746 MW; 1BA848F1CE95BC7D CRC64;
MKGTFFHNQR FLCFSILFMW IKTYVIYKLG FDLQIDTLLE ELMLLVNPLS FILPLFGIGL
FLKENKQRAF LLIANLVLTV ILISNTIFYG FYIDFITIPV LFQASNMSDM GSSVKELFHP
LFIALFVDLV FLLLFARKTK HPQTKAAPHT IKRYYAASCG MLLCTLALAE VQQPKLLAHS
FDREMLVKSI GLFQFHIYDT ISQTVNISAK AFADEDSITA IKNYTEADYS KPDQSKFGLA
KGRNVIFVTL ESTQSFVLNE KVNGKEITPF MNDLIKKSYS FDHFYQQTEQ GKTSDSEFIV
ANSLYPSLSG AVFFTKSDHQ FHTMYKSLKQ HDYYSAVFHA NHKTFWNRDV MYDTFGIDRF
FDVDDFHVTP GTSTSWGLKD KEFLEQSAKK LKSLPQPFYS SFITLTNHFP FEIDEKDQLI
DEFDSSSDLL NRYVTTVRYE DEALKHFIKK LKDEGLYENS MIVFMGDHYG ISEAHNEAMA
EFLGKDEITP YDNVQLQRVP FIIHIPGITD QQPETIPDAG GQVDVRPTLM HLLGVETKGD
IQFGNDLLSG DRTPFAVLRN GSFITNDYVY TKNTCYSQKT GEVLEDQDAC LPYKEKANEE
LSLSDKILNG DLLRFSE
