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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};
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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
 
 
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