Y067_CHLTR
ID Y067_CHLTR Reviewed; 326 AA.
AC Q9S529; O84070;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Uncharacterized metal-binding lipoprotein CT_067;
DE Flags: Precursor;
GN OrderedLocusNames=CT_067;
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 [GENOMIC DNA].
RC STRAIN=L2/434/Bu;
RX PubMed=10463174; DOI=10.1099/13500872-145-8-2077;
RA Bannantine J.P., Rockey D.D.;
RT "Use of primate model system to identify Chlamydia trachomatis protein
RT antigens recognized uniquely in the context of infection.";
RL Microbiology 145:2077-2085(1999).
RN [2]
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).
CC -!- FUNCTION: Part of an ATP-driven transport system
CC CT_067/CT_068/CT_069/CT_070 for a metal. Metal-binding component.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC35948.1; Type=Erroneous initiation; Evidence={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; AF077010; AAC35948.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE001273; AAC67658.1; -; Genomic_DNA.
DR PIR; E71561; E71561.
DR RefSeq; NP_219570.1; NC_000117.1.
DR RefSeq; WP_009871416.1; NC_000117.1.
DR PDB; 6NSI; X-ray; 2.00 A; A=40-326.
DR PDBsum; 6NSI; -.
DR AlphaFoldDB; Q9S529; -.
DR SMR; Q9S529; -.
DR STRING; 813.O172_00375; -.
DR EnsemblBacteria; AAC67658; AAC67658; CT_067.
DR GeneID; 884065; -.
DR KEGG; ctr:CT_067; -.
DR PATRIC; fig|272561.5.peg.76; -.
DR HOGENOM; CLU_016838_1_1_0; -.
DR InParanoid; Q9S529; -.
DR OMA; DPHIWFD; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005886; C:plasma membrane; 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:0030001; P:metal ion transport; IEA:InterPro.
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; Cell membrane; Lipoprotein; Membrane; Metal-binding;
KW Palmitate; Reference proteome; Signal; Transport.
FT SIGNAL 1..21
FT /evidence="ECO:0000305"
FT CHAIN 22..326
FT /note="Uncharacterized metal-binding lipoprotein CT_067"
FT /id="PRO_0000031901"
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 VARIANT 190
FT /note="A -> V (in strain: L2/434/Bu)"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:6NSI"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:6NSI"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:6NSI"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:6NSI"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 119..124
FT /evidence="ECO:0007829|PDB:6NSI"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 146..163
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 168..193
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:6NSI"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 221..226
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:6NSI"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:6NSI"
FT STRAND 298..300
FT /evidence="ECO:0007829|PDB:6NSI"
FT HELIX 305..319
FT /evidence="ECO:0007829|PDB:6NSI"
SQ SEQUENCE 326 AA; 37035 MW; 5A5AA35AB6627D89 CRC64;
MSFFHTRKYK LILRGLLCLA GCFLMNSCSS SRGNQPADES IYVLSMNRMI CDCVSRITGD
RVKNIVLIDG AIDPHSYEMV KGDEDRMAMS QLIFCNGLGL EHSASLRKHL EGNPKVVDLG
QRLLNKNCFD LLSEEGFPDP HIWTDMRVWG AAVKEMAAAL IQQFPQYEED FQKNADQILS
EMEELDRWAA RSLSTIPEKN RYLVTGHNAF SYFTRRYLSS DAERVSGEWR SRCISPEGLS
PEAQISIRDI MRVVEYISAN DVEVVFLEDT LNQDALRKIV SCSKSGQKIR LAKSPLYSDN
VCDNYFSTFQ HNVRTITEEL GGTVLE