TROA_TREPA
ID TROA_TREPA Reviewed; 308 AA.
AC P96116; Q56329;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Periplasmic zinc-binding protein TroA;
DE AltName: Full=Tromp-1;
DE Flags: Precursor;
GN Name=troA; Synonyms=troMP1; OrderedLocusNames=TP_0163;
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=7768866; DOI=10.1128/jb.177.12.3556-3562.1995;
RA Blanco D.R., Champion C.I., Exner M.M., Erdjument-Bromage H., Hancock R.E.,
RA Tempst P., Miller J.N., Lovett M.A.;
RT "Porin activity and sequence analysis of a 31-kilodalton Treponema pallidum
RT subsp. pallidum rare outer membrane protein (Tromp1).";
RL J. Bacteriol. 177:3556-3562(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9332349; DOI=10.1016/s0378-1119(97)00234-5;
RA Hardham J.M., Stamm L.V., Porcella S.F., Frye J.G., Barnes N.Y.,
RA Howell J.K., Mueller S.L., Radolf J.D., Weinstock G.M., Norris S.J.;
RT "Identification and transcriptional analysis of a Treponema pallidum operon
RT encoding a putative ABC transport system, an iron-activated repressor
RT protein homolog, and a glycolytic pathway enzyme homolog.";
RL Gene 197:47-64(1997).
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).
RN [4]
RP CHARACTERIZATION.
RX PubMed=10400603; DOI=10.1128/jb.181.14.4420-4423.1999;
RA Deka R.K., Lee Y.-H., Hagman K.E., Shevchenko D., Lingwood C.A.,
RA Hasemann C.A., Norgard M.V., Radolf J.D.;
RT "Physicochemical evidence that Treponema pallidum TroA is a zinc-containing
RT metalloprotein that lacks porin-like structure.";
RL J. Bacteriol. 181:4420-4423(1999).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-313.
RX PubMed=10404217; DOI=10.1038/10677;
RA Lee Y.-H., Deka R.K., Norgard M.V., Radolf J.D., Hasemann C.A.;
RT "Treponema pallidum TroA is a periplasmic zinc-binding protein with a
RT helical backbone.";
RL Nat. Struct. Biol. 6:628-633(1999).
CC -!- FUNCTION: Part of an ATP-driven transport system TroABCD for zinc.
CC Substrate-binding protein involved in the transport of zinc across the
CC cytoplasmic membrane.
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be an outer membrane protein with
CC porin-like properties. {ECO:0000305|PubMed:7768866}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA92353.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U16363; AAA92353.1; ALT_INIT; Genomic_DNA.
DR EMBL; U55214; AAC45725.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65151.1; -; Genomic_DNA.
DR PIR; A71360; A71360.
DR RefSeq; WP_010881610.1; NC_021490.2.
DR PDB; 1K0F; X-ray; 2.50 A; A=32-308.
DR PDB; 1TOA; X-ray; 1.80 A; A/B=23-308.
DR PDBsum; 1K0F; -.
DR PDBsum; 1TOA; -.
DR AlphaFoldDB; P96116; -.
DR SMR; P96116; -.
DR IntAct; P96116; 8.
DR STRING; 243276.TPANIC_0163; -.
DR TCDB; 3.A.1.15.8; the atp-binding cassette (abc) superfamily.
DR EnsemblBacteria; AAC65151; AAC65151; TP_0163.
DR GeneID; 57878705; -.
DR KEGG; tpa:TP_0163; -.
DR eggNOG; COG0803; Bacteria.
DR HOGENOM; CLU_016838_1_1_12; -.
DR OMA; DPHIWFD; -.
DR OrthoDB; 1703187at2; -.
DR EvolutionaryTrace; P96116; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0006829; P:zinc ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR006129; AdhesinB.
DR InterPro; IPR006128; Lipoprotein_4.
DR InterPro; IPR006127; ZnuA-like.
DR Pfam; PF01297; ZnuA; 1.
DR PRINTS; PR00691; ADHESINB.
DR PRINTS; PR00690; ADHESNFAMILY.
PE 1: Evidence at protein level;
KW 3D-structure; Ion transport; Metal-binding; Periplasm; Reference proteome;
KW Signal; Transport; Zinc; Zinc transport.
FT SIGNAL 1..22
FT CHAIN 23..308
FT /note="Periplasmic zinc-binding protein TroA"
FT /id="PRO_0000031872"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 41..51
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:1TOA"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1TOA"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:1TOA"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1TOA"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:1K0F"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:1K0F"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:1TOA"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 113..116
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1TOA"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1K0F"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 138..155
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 160..186
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1TOA"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 203..209
FT /evidence="ECO:0007829|PDB:1TOA"
FT STRAND 212..217
FT /evidence="ECO:0007829|PDB:1TOA"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1K0F"
FT HELIX 227..239
FT /evidence="ECO:0007829|PDB:1TOA"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:1TOA"
FT TURN 265..267
FT /evidence="ECO:0007829|PDB:1TOA"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:1TOA"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:1TOA"
FT HELIX 291..306
FT /evidence="ECO:0007829|PDB:1TOA"
SQ SEQUENCE 308 AA; 33570 MW; 2FDD8FF20D012B08 CRC64;
MIRERICACV LALGMLTGFT HAFGSKDAAA DGKPLVVTTI GMIADAVKNI AQGDVHLKGL
MGPGVDPHLY TATAGDVEWL GNADLILYNG LHLETKMGEV FSKLRGSRLV VAVSETIPVS
QRLSLEEAEF DPHVWFDVKL WSYSVKAVYE SLCKLLPGKT REFTQRYQAY QQQLDKLDAY
VRRKAQSLPA ERRVLVTAHD AFGYFSRAYG FEVKGLQGVS TASEASAHDM QELAAFIAQR
KLPAIFIESS IPHKNVEALR DAVQARGHVV QIGGELFSDA MGDAGTSEGT YVGMVTHNID
TIVAALAR
