ARTJ_CHLTR
ID ARTJ_CHLTR Reviewed; 257 AA.
AC O84385;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable ABC transporter arginine-binding protein ArtJ;
DE Flags: Precursor;
GN Name=artJ; OrderedLocusNames=CT_381;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 24-257, FUNCTION, SUBCELLULAR
RP LOCATION, AND SPECIES-SPECIFIC IMMUNOGENICITY.
RC STRAIN=D/UW-3/Cx;
RX PubMed=20592031; DOI=10.1074/jbc.m110.118513;
RA Soriani M., Petit P., Grifantini R., Petracca R., Gancitano G.,
RA Frigimelica E., Nardelli F., Garcia C., Spinelli S., Scarabelli G.,
RA Fiorucci S., Affentranger R., Ferrer-Navarro M., Zacharias M., Colombo G.,
RA Vuillard L., Daura X., Grandi G.;
RT "Exploiting antigenic diversity for vaccine design: the chlamydia ArtJ
RT paradigm.";
RL J. Biol. Chem. 285:30126-30138(2010).
CC -!- FUNCTION: Probably part of an ABC transporter complex involved in
CC arginine transport. Binds arginine (By similarity). Interacts with host
CC epithelial cells, suggesting a role in host-cell adhesion during
CC infection. {ECO:0000250, ECO:0000269|PubMed:20592031}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20592031}. Cell
CC surface {ECO:0000269|PubMed:20592031}.
CC -!- MISCELLANEOUS: Does not induce neutralizing antibodies.
CC -!- MISCELLANEOUS: This protein, although well conserved among chlamydial
CC species, shows species-specific immunogenicity.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001273; AAC67977.1; -; Genomic_DNA.
DR PIR; A71522; A71522.
DR RefSeq; NP_219890.1; NC_000117.1.
DR RefSeq; WP_009871733.1; NC_000117.1.
DR PDB; 3DEL; X-ray; 1.92 A; B/C/D/F=24-257.
DR PDBsum; 3DEL; -.
DR AlphaFoldDB; O84385; -.
DR SMR; O84385; -.
DR STRING; 813.O172_02075; -.
DR EnsemblBacteria; AAC67977; AAC67977; CT_381.
DR GeneID; 884734; -.
DR KEGG; ctr:CT_381; -.
DR PATRIC; fig|272561.5.peg.410; -.
DR HOGENOM; CLU_019602_18_2_0; -.
DR InParanoid; O84385; -.
DR OMA; DTPFENF; -.
DR EvolutionaryTrace; O84385; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR CDD; cd00999; PBP2_ArtJ; 1.
DR InterPro; IPR037297; ArtJ_PBP2.
DR InterPro; IPR001638; Solute-binding_3/MltF_N.
DR Pfam; PF00497; SBP_bac_3; 1.
DR SMART; SM00062; PBPb; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Reference proteome; Secreted; Signal;
KW Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..257
FT /note="Probable ABC transporter arginine-binding protein
FT ArtJ"
FT /id="PRO_0000383474"
FT BINDING 41
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250"
FT BINDING 99..102
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000250"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:3DEL"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 111..130
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 144..147
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 170..178
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 181..187
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3DEL"
FT STRAND 215..223
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 227..242
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 245..252
FT /evidence="ECO:0007829|PDB:3DEL"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3DEL"
SQ SEQUENCE 257 AA; 28629 MW; 5681A1BB8F6957CA CRC64;
MCIKRKKTWI AFLAVVCSFC LTGCLKEGGD SNSEKFIVGT NATYPPFEFV DKRGEVVGFD
IDLAREISNK LGKTLDVREF SFDALILNLK QHRIDAVITG MSITPSRLKE ILMIPYYGEE
IKHLVLVFKG ENKHPLPLTQ YRSVAVQTGT YQEAYLQSLS EVHIRSFDST LEVLMEVMHG
KSPVAVLEPS IAQVVLKDFP ALSTATIDLP EDQWVLGYGI GVASDRPALA LKIEAAVQEI
RKEGVLAELE QKWGLNN
