INCG_CHLT2
ID INCG_CHLT2 Reviewed; 167 AA.
AC A0A0H3MGR4; O84120; Q9RPP8;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Inclusion membrane protein G {ECO:0000303|PubMed:10447885};
GN Name=incG {ECO:0000303|PubMed:10447885}; OrderedLocusNames=CTL0373;
OS Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=471472;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=10447885; DOI=10.1046/j.1365-2958.1999.01523.x;
RA Scidmore-Carlson M.A., Shaw E.I., Dooley C.A., Fischer E.R., Hackstadt T.;
RT "Identification and characterization of a Chlamydia trachomatis early
RT operon encoding four novel inclusion membrane proteins.";
RL Mol. Microbiol. 33:753-765(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=18032721; DOI=10.1101/gr.7020108;
RA Thomson N.R., Holden M.T.G., Carder C., Lennard N., Lockey S.J., Marsh P.,
RA Skipp P., O'Connor C.D., Goodhead I., Norbertzcak H., Harris B., Ormond D.,
RA Rance R., Quail M.A., Parkhill J., Stephens R.S., Clarke I.N.;
RT "Chlamydia trachomatis: genome sequence analysis of lymphogranuloma
RT venereum isolates.";
RL Genome Res. 18:161-171(2008).
RN [3]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=11207546; DOI=10.1046/j.1462-5822.1999.00012.x;
RA Hackstadt T., Scidmore-Carlson M.A., Shaw E.I., Fischer E.R.;
RT "The Chlamydia trachomatis IncA protein is required for homotypic vesicle
RT fusion.";
RL Cell. Microbiol. 1:119-130(1999).
RN [4]
RP INTERACTION WITH HUMAN 14-3-3 BETA, SUBCELLULAR LOCATION, PROBABLE
RP PHOSPHORYLATION AT SER-166, DOMAIN, AND MUTAGENESIS OF SER-164 AND SER-166.
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=11260479; DOI=10.1046/j.1365-2958.2001.02355.x;
RA Scidmore M.A., Hackstadt T.;
RT "Mammalian 14-3-3beta associates with the Chlamydia trachomatis inclusion
RT membrane via its interaction with IncG.";
RL Mol. Microbiol. 39:1638-1650(2001).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=12065525; DOI=10.1128/iai.70.7.3816-3823.2002;
RA Fields K.A., Fischer E.R., Hackstadt T.;
RT "Inhibition of fusion of Chlamydia trachomatis inclusions at 32 degrees C
RT correlates with restricted export of IncA.";
RL Infect. Immun. 70:3816-3823(2002).
RN [6]
RP INTERACTION WITH PKN1, AND PHOSPHORYLATION BY PKN1.
RC STRAIN=L2;
RX PubMed=14500499; DOI=10.1128/iai.71.10.5772-5784.2003;
RA Verma A., Maurelli A.T.;
RT "Identification of two eukaryote-like serine/threonine kinases encoded by
RT Chlamydia trachomatis serovar L2 and characterization of interacting
RT partners of Pkn1.";
RL Infect. Immun. 71:5772-5784(2003).
RN [7]
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION, AND PROBABLE EXPORT
RP BY A TYPE III SECRETION SYSTEM.
RC STRAIN=L2;
RX PubMed=12694613; DOI=10.1046/j.1365-2958.2003.03462.x;
RA Fields K.A., Mead D.J., Dooley C.A., Hackstadt T.;
RT "Chlamydia trachomatis type III secretion: evidence for a functional
RT apparatus during early-cycle development.";
RL Mol. Microbiol. 48:671-683(2003).
CC -!- FUNCTION: Inclusion membrane protein probably involved in early
CC modification events of the chlamydial inclusion.
CC {ECO:0000305|PubMed:10447885}.
CC -!- SUBUNIT: In infected HeLa cells colocalizes with host 14-3-3 protein
CC (YWHAB); phosphorylation of Ser-166 is probably required
CC (PubMed:11260479). Interacts with Pkn1 (PubMed:14500499).
CC {ECO:0000269|PubMed:11260479, ECO:0000269|PubMed:14500499}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:10447885}. Host
CC vacuole, host pathogen-containing vacuole, host pathogen-containing
CC vacuole membrane {ECO:0000269|PubMed:10447885,
CC ECO:0000269|PubMed:11207546, ECO:0000269|PubMed:12065525}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Secreted, probably by a type III
CC secretion system (Probable). Localized in the inclusion membrane
CC (PubMed:10447885, PubMed:11207546, PubMed:11260479, PubMed:12065525).
CC Inclusion membrane staining is punctate (PubMed:10447885). The C-
CC terminus faces the host cytosol (PubMed:11207546).
CC {ECO:0000269|PubMed:10447885, ECO:0000269|PubMed:11207546,
CC ECO:0000269|PubMed:11260479, ECO:0000269|PubMed:12065525,
CC ECO:0000305|PubMed:10447885, ECO:0000305|PubMed:12694613}.
CC -!- DEVELOPMENTAL STAGE: Present in reticulate bodies (RB) not detected in
CC elementary bodies (EB) (at protein level) (PubMed:10447885). Found only
CC in reticulate bodies in infected HeLa cells (PubMed:12694613).
CC {ECO:0000269|PubMed:10447885, ECO:0000269|PubMed:12694613}.
CC -!- INDUCTION: Cotranscribed with incD, incE and incG within 2 hours after
CC internalization by host cells (PubMed:10447885). Detected at 4 hours
CC post-infection in HeLa cells (at protein level) (PubMed:12694613).
CC {ECO:0000269|PubMed:10447885, ECO:0000269|PubMed:12694613}.
CC -!- PTM: Phosphorylated, possibly at more than one position, in infected
CC HeLa cells (PubMed:11260479). Phosphorylated by chlamydial kinase Pnk1
CC (PubMed:14500499). {ECO:0000269|PubMed:11260479,
CC ECO:0000269|PubMed:14500499}.
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; AF151374; AAD43977.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP03813.1; -; Genomic_DNA.
DR RefSeq; WP_009873573.1; NC_010287.1.
DR RefSeq; YP_001654457.1; NC_010287.1.
DR AlphaFoldDB; A0A0H3MGR4; -.
DR iPTMnet; A0A0H3MGR4; -.
DR EnsemblBacteria; CAP03813; CAP03813; CTL0373.
DR KEGG; ctb:CTL0373; -.
DR PATRIC; fig|471472.4.peg.405; -.
DR HOGENOM; CLU_1701112_0_0_0; -.
DR OMA; PESIPMS; -.
DR Proteomes; UP000000795; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0140221; C:pathogen-containing vacuole membrane; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Host membrane; Membrane; Phosphoprotein; Secreted; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..167
FT /note="Inclusion membrane protein G"
FT /id="PRO_0000446191"
FT TRANSMEM 33..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 94..167
FT /note="Sufficient for interaction with human 14-3-3 beta
FT protein"
FT /evidence="ECO:0000269|PubMed:11260479"
FT REGION 97..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..166
FT /note="Phosphorylation-dependent binding motif"
FT /evidence="ECO:0000305|PubMed:11260479"
FT COMPBIAS 113..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 166
FT /note="Interacts with 14-3-3 beta"
FT /evidence="ECO:0000305|PubMed:11260479"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000305|PubMed:11260479"
FT MUTAGEN 164
FT /note="S->A: 2 to 3-fold decrease of in vitro binding to
FT 14-3-3 beta."
FT /evidence="ECO:0000269|PubMed:11260479"
FT MUTAGEN 166
FT /note="S->A: Loss of binding to 14-3-3 beta in vitro."
FT /evidence="ECO:0000269|PubMed:11260479"
SQ SEQUENCE 167 AA; 17540 MW; DF2977343B8DC16E CRC64;
MICCDKVLSS VQSMPVIDKC SVTKCLQTAK QAVVLALSLF AVFASGSLSI LSAAVLFSGT
AAVLPYLLIL TTALLGCVYA VIVLLRSLSA VVQSCKKRSP EEIEGAARPS DQQESGGRLS
EESASPQASP TSSTLRLESA FRSIGDSVSG AFDDINKDNS RSRSRSF
