ID   INCG_CHLTR              Reviewed;         167 AA.
AC   P0DPS6; O84120; Q9RPP8;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Inclusion membrane protein G;
GN   Name=incG; OrderedLocusNames=CT_118;
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   SUBCELLULAR LOCATION.
RC   STRAIN=D/UW-3/Cx;
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   [3]
RP   INTERACTION WITH 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).
CC   -!- FUNCTION: Inclusion membrane protein probably involved in early
CC       modification events of the chlamydial inclusion (By similarity). Binds
CC       to the host cell 14-3-3 beta (YWHAB); phosphorylation of Ser-166 is
CC       probably required (By similarity). {ECO:0000250|UniProtKB:A0A0H3MGR4}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A0H3MGR4}. Host
CC       vacuole, host pathogen-containing vacuole, host pathogen-containing
CC       vacuole membrane {ECO:0000305|PubMed:11260479}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=Secreted, probably by a type III secretion
CC       system (By similarity). Localized in the inclusion membrane (By
CC       similarity). {ECO:0000250|UniProtKB:A0A0H3MGR4}.
CC   -!- PTM: Phosphorylated by chlamydial kinase Pnk1.
CC       {ECO:0000269|PubMed:11260479}.
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DR   EMBL; AE001273; AAC67709.1; -; Genomic_DNA.
DR   PIR; B71553; B71553.
DR   RefSeq; NP_219621.1; NC_000117.1.
DR   RefSeq; WP_009871465.1; NC_000117.1.
DR   AlphaFoldDB; P0DPS6; -.
DR   IntAct; P0DPS6; 1.
DR   MINT; P0DPS6; -.
DR   STRING; 813.O172_00640; -.
DR   EnsemblBacteria; AAC67709; AAC67709; CT_118.
DR   GeneID; 884170; -.
DR   KEGG; ctr:CT_118; -.
DR   OMA; PESIPMS; -.
DR   Proteomes; UP000000431; 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; Reference proteome; Secreted;
KW   Transmembrane; Transmembrane helix; Virulence.
FT   CHAIN           1..167
FT                   /note="Inclusion membrane protein G"
FT                   /id="PRO_0000084204"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          97..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          148..167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           161..166
FT                   /note="Phosphorylation-dependent binding motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3MGR4"
FT   COMPBIAS        113..136
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:0000250|UniProtKB:A0A0H3MGR4"
FT   MOD_RES         166
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:A0A0H3MGR4"
SQ   SEQUENCE   167 AA;  17405 MW;  CB720C45F3A713E4 CRC64;
     MICCDKVLSS VQSMPVIDKC SVTKCLQTAK QAAVLALSLF AVFASGSLSI LSAAVLFSGT
     AAVLPYLLIL TTALLGFVCA VIVLLRNLSA VVQSCKKRSP EEIEGAARPS DQQESGGRLS
     EESASPQASP TSSTFGLESA LRSIGDSVSG AFDDINKDNS RSRSHSF