MGLB_TREPA
ID MGLB_TREPA Reviewed; 403 AA.
AC Q08255;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Glucose/galactose-binding lipoprotein;
DE Flags: Precursor;
GN Name=mglB; Synonyms=tpp38; OrderedLocusNames=TP_0684;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=8132345; DOI=10.1128/iai.62.4.1381-1391.1994;
RA Becker P.S., Akins D.R., Radolf J.D., Norgard M.V.;
RT "Similarity between the 38-kilodalton lipoprotein of Treponema pallidum and
RT the glucose/galactose-binding (MglB) protein of Escherichia coli.";
RL Infect. Immun. 62:1381-1391(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=8921855; DOI=10.1016/0378-1119(96)00286-7;
RA Porcella S.F., Popova T.G., Hagman K.E., Penn C.W., Radolf J.D.,
RA Norgard M.V.;
RT "A mgl-like operon in Treponema pallidum, the syphilis spirochete.";
RL Gene 177:115-121(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- FUNCTION: May be involved in the transport of sugars. May have a role
CC in chemotaxis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; L20301; AAA27473.1; -; Genomic_DNA.
DR EMBL; U48416; AAC44584.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65647.1; -; Genomic_DNA.
DR PIR; JC5171; JC5171.
DR RefSeq; WP_010882129.1; NC_021490.2.
DR PDB; 5JX2; X-ray; 2.05 A; A=36-403.
DR PDB; 6BGC; X-ray; 2.08 A; A/B=36-403.
DR PDB; 6BGD; X-ray; 1.47 A; A=36-403.
DR PDBsum; 5JX2; -.
DR PDBsum; 6BGC; -.
DR PDBsum; 6BGD; -.
DR AlphaFoldDB; Q08255; -.
DR SMR; Q08255; -.
DR IntAct; Q08255; 15.
DR STRING; 243276.TPANIC_0684; -.
DR EnsemblBacteria; AAC65647; AAC65647; TP_0684.
DR KEGG; tpa:TP_0684; -.
DR eggNOG; COG1879; Bacteria.
DR HOGENOM; CLU_057130_0_0_12; -.
DR OMA; HNDSKAR; -.
DR OrthoDB; 351138at2; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR InterPro; IPR040740; MglB-2_Peripla_BP.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR Pfam; PF18610; Peripla_BP_7; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Sugar transport; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 26..403
FT /note="Glucose/galactose-binding lipoprotein"
FT /id="PRO_0000031743"
FT LIPID 26
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 26
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:6BGD"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 76..90
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 100..109
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 115..127
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 150..161
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 172..186
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 223..230
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 263..267
FT /evidence="ECO:0007829|PDB:6BGD"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:6BGD"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 325..333
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 337..341
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 368..372
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 378..380
FT /evidence="ECO:0007829|PDB:6BGD"
FT STRAND 382..386
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 394..398
FT /evidence="ECO:0007829|PDB:6BGD"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:6BGD"
SQ SEQUENCE 403 AA; 43052 MW; 2E05AF844EB8C5FD CRC64;
MKENSCTACS RRLALFVGAA VLVVGCSSKT DVTLNRDKPL VFFNRQPSDP LTGKVDMAAM
NWNDKTYYVG FDAKFGGSIQ GKMILDFLAS SESSVDRNGD GIIGYVLCIG DVGHNDSKVR
TEGIRRALGT WTGSSDPGQA KEGQAVVGGK SYKVVELEGK AMTGTDGSTW NTNSATESMG
SWVAKFADKI DLVISNNDGM AMGCLQASNY PRGLPIFGYD ANADAVESVG KGELTGTVSQ
NVDAQAVAVL QIIRNLLDGS SGEDVVANGI SRPDAHGNKI SAPVQYWEDV KAIMADNSEV
TSANWKEYTR GARDAGVRQV SAPTKKVLLT VHNASNDFLA SAYLPALKHY APLLNVDLTV
VQGDGQNELS CLDKFTNLDM FDAFAVNMVK TNSGADYTDK LKY
