OUTS_DICD3
ID OUTS_DICD3 Reviewed; 133 AA.
AC Q01567; E0SM45;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Pilotin OutS;
DE AltName: Full=Lipoprotein OutS;
DE Flags: Precursor;
GN Name=outS; OrderedLocusNames=Dda3937_02411;
OS Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Dickeya.
OX NCBI_TaxID=198628;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=1453958; DOI=10.1111/j.1365-2958.1992.tb01775.x;
RA Condemine G., Dorel C., Hugouvieux-Cotte-Pattat N., Robert-Baudouy J.;
RT "Some of the out genes involved in the secretion of pectate lyases in
RT Erwinia chrysanthemi are regulated by kdgR.";
RL Mol. Microbiol. 6:3199-3211(1992).
RN [2]
RP SEQUENCE REVISION.
RA Condemine G.;
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3937;
RX PubMed=21217001; DOI=10.1128/jb.01513-10;
RA Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T., Expert D.,
RA Plunkett G. III, San Francisco M.J., Charkowski A.O., Py B., Bell K.,
RA Rauscher L., Rodriguez-Palenzuela P., Toussaint A., Holeva M.C., He S.Y.,
RA Douet V., Boccara M., Blanco C., Toth I., Anderson B.D., Biehl B.S.,
RA Mau B., Flynn S.M., Barras F., Lindeberg M., Birch P.R., Tsuyumu S.,
RA Shi X., Hibbing M., Yap M.N., Carpentier M., Dassa E., Umehara M.,
RA Kim J.F., Rusch M., Soni P., Mayhew G.F., Fouts D.E., Gill S.R.,
RA Blattner F.R., Keen N.T., Perna N.T.;
RT "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii 3937.";
RL J. Bacteriol. 193:2076-2077(2011).
RN [4] {ECO:0007744|PDB:4K0U}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 28-133, SUBUNIT, AND DISULFIDE
RP BOND.
RX PubMed=23897461; DOI=10.1107/s0907444913007658;
RA Rehman S., Gu S., Shevchik V.E., Pickersgill R.W.;
RT "Anatomy of secretin binding to the Dickeya dadantii type II secretion
RT system pilotin.";
RL Acta Crystallogr. D 69:1381-1386(2013).
CC -!- FUNCTION: Out proteins are required for the translocation of pectate
CC lyases and cellulases across the outer membrane.
CC -!- SUBUNIT: Interacts with secretin OutD. {ECO:0000269|PubMed:23897461}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC -!- SIMILARITY: To K.pneumoniae PulS. {ECO:0000305}.
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DR EMBL; X65265; CAA46372.1; -; Genomic_DNA.
DR EMBL; CP002038; ADM99380.1; -; Genomic_DNA.
DR PIR; S28011; S28011.
DR RefSeq; WP_013318814.1; NC_014500.1.
DR PDB; 3UTK; X-ray; 1.65 A; A/B=1-133.
DR PDB; 4K0U; X-ray; 2.15 A; A=28-133.
DR PDBsum; 3UTK; -.
DR PDBsum; 4K0U; -.
DR AlphaFoldDB; Q01567; -.
DR SMR; Q01567; -.
DR STRING; 198628.Dda3937_02411; -.
DR TCDB; 8.A.2.1.2; the secretin auxiliary lipoprotein (sal) family.
DR EnsemblBacteria; ADM99380; ADM99380; Dda3937_02411.
DR GeneID; 9734629; -.
DR KEGG; ddd:Dda3937_02411; -.
DR PATRIC; fig|198628.6.peg.3141; -.
DR eggNOG; ENOG5032UQ7; Bacteria.
DR HOGENOM; CLU_154567_0_0_6; -.
DR OMA; PFIDAMR; -.
DR OrthoDB; 1568703at2; -.
DR BioCyc; DDAD198628:DDA3937_RS14820-MON; -.
DR Proteomes; UP000006859; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:ASAP.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016485; P:protein processing; IDA:ASAP.
DR Gene3D; 1.20.58.1630; -; 1.
DR InterPro; IPR005699; Chap_lipoprot_PulS/OutS.
DR InterPro; IPR019114; Chap_lipoprot_PulS/OutS-like.
DR InterPro; IPR038432; PulS/OutS-like_sf.
DR Pfam; PF09691; T2SS_PulS_OutS; 1.
DR TIGRFAMs; TIGR01004; PulS_OutS; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Disulfide bond; Lipoprotein; Membrane;
KW Palmitate; Protein transport; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000305"
FT CHAIN 21..133
FT /note="Pilotin OutS"
FT /id="PRO_0000018184"
FT LIPID 21
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 21
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT DISULFID 61..115
FT /evidence="ECO:0000269|PubMed:23897461"
FT HELIX 40..60
FT /evidence="ECO:0007829|PDB:3UTK"
FT HELIX 69..82
FT /evidence="ECO:0007829|PDB:3UTK"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:4K0U"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:3UTK"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:3UTK"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:3UTK"
SQ SEQUENCE 133 AA; 14334 MW; 5948CEAEA124E9CB CRC64;
MHVSSLKVVL FGVCCLSLAA CQTPAPVKNT ASRSAASVPA NEQISQLASL VAASKYLRVQ
CERSDLPDDG TILKTAVNVA VQKGWDTGRY QSLPQLSENL YQGLLKDGTP KATQCSSFNR
TMTPFLDAMR TVR
