P22_BORBU
ID P22_BORBU Reviewed; 194 AA.
AC P0CL67; P0C924; Q05903; Q45008;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Outer surface 22 kDa lipoprotein;
DE AltName: Full=Antigen IPLA7;
DE Flags: Precursor;
GN Name=p22; OrderedLocusNames=BB_0365;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.
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DR EMBL; AE000783; AAC66748.1; -; Genomic_DNA.
DR PIR; D70145; D70145.
DR RefSeq; NP_212499.1; NC_001318.1.
DR RefSeq; WP_002657819.1; NC_001318.1.
DR PDB; 6R1G; X-ray; 1.55 A; A/B=28-194.
DR PDBsum; 6R1G; -.
DR AlphaFoldDB; P0CL67; -.
DR SMR; P0CL67; -.
DR EnsemblBacteria; AAC66748; AAC66748; BB_0365.
DR GeneID; 56567793; -.
DR KEGG; bbu:BB_0365; -.
DR PATRIC; fig|224326.49.peg.760; -.
DR HOGENOM; CLU_1400113_0_0_12; -.
DR OMA; VHSKNDR; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IDA:CAFA.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000305"
FT CHAIN 22..194
FT /note="Outer surface 22 kDa lipoprotein"
FT /id="PRO_0000018085"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:6R1G"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:6R1G"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:6R1G"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:6R1G"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:6R1G"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:6R1G"
FT STRAND 107..116
FT /evidence="ECO:0007829|PDB:6R1G"
FT STRAND 119..127
FT /evidence="ECO:0007829|PDB:6R1G"
FT STRAND 131..142
FT /evidence="ECO:0007829|PDB:6R1G"
FT HELIX 145..148
FT /evidence="ECO:0007829|PDB:6R1G"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:6R1G"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:6R1G"
FT HELIX 169..188
FT /evidence="ECO:0007829|PDB:6R1G"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:6R1G"
SQ SEQUENCE 194 AA; 21866 MW; D42A7CE0E26811B6 CRC64;
MYKNGFFKNY LSLFLIFLVI ACTSKDSSNE YVEEQEAENS SKPDDSKIDE HTIGHVFHAM
GVVHSKKDRK SLGKNIKVFY FSEEDGHFQT IPSKENAKLI VYFYDNVYAG EAPISISGKE
AFIFVGITPD FKKIINSNLH GAKSDLIGTF KDLNIKNSKL EITVDENNSD AKTFLESVNY
IIDGVEKISP MLTN