ARTJ_CHLPN
ID ARTJ_CHLPN Reviewed; 259 AA.
AC Q9Z869; Q7AIQ4; Q7VQ00; Q9JS59;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Probable ABC transporter arginine-binding protein ArtJ;
DE Flags: Precursor;
GN Name=artJ; OrderedLocusNames=CPn_0482, CP_0272, CPj0482, CpB0502;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, AND BIOTECHNOLOGY.
RC STRAIN=FB/96;
RX PubMed=15629361; DOI=10.1016/j.vaccine.2004.07.045;
RA Finco O., Bonci A., Agnusdei M., Scarselli M., Petracca R., Norais N.,
RA Ferrari G., Garaguso I., Donati M., Sambri V., Cevenini R., Ratti G.,
RA Grandi G.;
RT "Identification of new potential vaccine candidates against Chlamydia
RT pneumoniae by multiple screenings.";
RL Vaccine 23:1178-1188(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 23-259 IN COMPLEX WITH ARGININE,
RP FUNCTION, AND SPECIES-SPECIFIC IMMUNOGENICITY.
RC STRAIN=FB/96;
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. Interacts with host epithelial
CC cells, suggesting a role in host-cell adhesion during infection.
CC {ECO:0000269|PubMed:20592031}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15629361}. Cell
CC surface {ECO:0000269|PubMed:15629361}.
CC -!- BIOTECHNOLOGY: Was identified as a potential vaccine component. In
CC vitro, induces antibodies capable of neutralizing the infectivity of
CC C.pneumoniae. {ECO:0000269|PubMed:15629361}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAP98431.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE001363; AAD18622.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38132.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA98688.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98431.1; ALT_INIT; Genomic_DNA.
DR PIR; F72073; F72073.
DR PIR; F86550; F86550.
DR PIR; G81595; G81595.
DR RefSeq; NP_224678.1; NC_000922.1.
DR RefSeq; WP_010883120.1; NZ_LN847257.1.
DR PDB; 3N26; X-ray; 2.10 A; A=23-259.
DR PDB; 3QAX; X-ray; 2.00 A; A/B=1-259.
DR PDBsum; 3N26; -.
DR PDBsum; 3QAX; -.
DR AlphaFoldDB; Q9Z869; -.
DR SMR; Q9Z869; -.
DR STRING; 115711.CP_0272; -.
DR EnsemblBacteria; AAD18622; AAD18622; CPn_0482.
DR EnsemblBacteria; AAF38132; AAF38132; CP_0272.
DR GeneID; 45050527; -.
DR KEGG; cpa:CP_0272; -.
DR KEGG; cpj:artJ; -.
DR KEGG; cpn:CPn_0482; -.
DR KEGG; cpt:CpB0502; -.
DR PATRIC; fig|115713.3.peg.540; -.
DR eggNOG; COG0834; Bacteria.
DR HOGENOM; CLU_019602_18_2_0; -.
DR OrthoDB; 847343at2; -.
DR EvolutionaryTrace; Q9Z869; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid transport; Secreted; Signal; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 26..259
FT /note="Probable ABC transporter arginine-binding protein
FT ArtJ"
FT /id="PRO_0000403377"
FT BINDING 38
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:20592031"
FT BINDING 96..99
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT BINDING 104
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:20592031"
FT BINDING 149
FT /ligand="L-arginine"
FT /ligand_id="ChEBI:CHEBI:32682"
FT /evidence="ECO:0000269|PubMed:20592031"
FT VARIANT 139
FT /note="Y -> H (in strain: AR39 and J138)"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3QAX"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 82..87
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 120..126
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:3QAX"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 225..240
FT /evidence="ECO:0007829|PDB:3QAX"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:3QAX"
SQ SEQUENCE 259 AA; 29070 MW; 14B29689F827419E CRC64;
MIKQIGRFFR AFIFIMPLSL TSCESKIDRN RIWIVGTNAT YPPFEYVDAQ GEVVGFDIDL
AKAISEKLGK QLEVREFAFD ALILNLKKHR IDAILAGMSI TPSRQKEIAL LPYYGDEVQE
LMVVSKRSLE TPVLPLTQYS SVAVQTGTFQ EHYLLSQPGI CVRSFDSTLE VIMEVRYGKS
PVAVLEPSVG RVVLKDFPNL VATRLELPPE CWVLGCGLGV AKDRPEEIQT IQQAITDLKS
EGVIQSLTKK WQLSEVAYE
