INCA_CHLT2
ID INCA_CHLT2 Reviewed; 273 AA.
AC A0A0H3MD02; O69196; Q9AMA4; Q9AMA5; Q9AMA6; Q9AMB2;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2019, sequence version 2.
DT 03-AUG-2022, entry version 29.
DE RecName: Full=Inclusion membrane protein A;
GN Name=incA; OrderedLocusNames=CTL0374;
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], AND SUBCELLULAR LOCATION.
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=9826388; DOI=10.1128/iai.66.12.6017-6021.1998;
RA Bannantine J.P., Stamm W.E., Suchland R.J., Rockey D.D.;
RT "Chlamydia trachomatis IncA is localized to the inclusion membrane and is
RT recognized by antisera from infected humans and primates.";
RL Infect. Immun. 66:6017-6021(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=11402010; DOI=10.1128/iai.69.7.4654-4656.2001;
RA Pannekoek Y., van der Ende A., Eijk P.P., van Marle J., de Witte M.A.,
RA Ossewaarde J.M., van den Brule A.J.C., Morre S.A., Dankert J.;
RT "Normal IncA expression and fusogenicity of inclusions in Chlamydia
RT trachomatis isolates with the incA I47T mutation.";
RL Infect. Immun. 69:4654-4656(2001).
RN [3]
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 [4]
RP FUNCTION, SUBUNIT, 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 [5]
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 [6]
RP INHIBITION OF SECRETION.
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 [7]
RP PROBABLE EXPORT 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).
RN [8]
RP SUBUNIT, OLIGOMERIZATION, AND DOMAIN.
RC STRAIN=434/Bu / ATCC VR-902B;
RX PubMed=15316015; DOI=10.1074/jbc.m407227200;
RA Delevoye C., Nilges M., Dautry-Varsat A., Subtil A.;
RT "Conservation of the biochemical properties of IncA from Chlamydia
RT trachomatis and Chlamydia caviae: oligomerization of IncA mediates
RT interaction between facing membranes.";
RL J. Biol. Chem. 279:46896-46906(2004).
CC -!- FUNCTION: Chlamydia replicate within a host intracellular vacuole,
CC termed an inclusion, which is formed by fusion of many smaller
CC inclusion bodies. IncA may be involved in the homotypic fusion of
CC inclusions; injection of anti-IncA antibodies prevents homotypic
CC fusion, but not fusion with exocytic vesicles.
CC {ECO:0000269|PubMed:11207546}.
CC -!- SUBUNIT: May form homodimers via its C-terminus (PubMed:11207546).
CC Forms homodimers, and probably higher-order oligomers
CC (PubMed:15316015). {ECO:0000269|PubMed:11207546,
CC ECO:0000269|PubMed:15316015}.
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:9826388, ECO:0000305|PubMed:11402010}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Secreted, probably by a type III
CC secretion system (Probable). Secretion into the host pathogen-
CC containing vacuole membrane (inclusion body) is considerably decreased
CC when infected HeLa cells are grown at 32 degrees Celsius
CC (PubMed:12065525). Localized in the inclusion membrane (PubMed:9826388,
CC PubMed:11207546) (Probable). Inclusion membrane staining is punctate
CC (PubMed:10447885). In the inclusion, the C-terminus faces the host
CC cytosol (PubMed:11207546). {ECO:0000269|PubMed:10447885,
CC ECO:0000269|PubMed:11207546, ECO:0000269|PubMed:12065525,
CC ECO:0000269|PubMed:9826388, ECO:0000305|PubMed:11402010,
CC ECO:0000305|PubMed:12694613}.
CC -!- DEVELOPMENTAL STAGE: Present in reticulate bodies (RB) and much less in
CC elementary bodies (EB) (at protein level).
CC {ECO:0000269|PubMed:10447885}.
CC -!- INDUCTION: Detected 12 hours post-infection of host HeLa cells.
CC {ECO:0000269|PubMed:10447885}.
CC -!- DOMAIN: IncA proteins share the same general organization: a short N-
CC terminal domain, a large bilobed hydrophobic domain, and a C-terminal
CC cytoplasmic domain. {ECO:0000305|PubMed:15316015}.
CC -!- SIMILARITY: Belongs to the IncA family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAP03814.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF067958; AAC82641.1; -; Genomic_DNA.
DR EMBL; AF327009; AAG61106.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP03814.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_009873574.1; NC_010287.1.
DR RefSeq; YP_001654458.1; NC_010287.1.
DR AlphaFoldDB; A0A0H3MD02; -.
DR SMR; A0A0H3MD02; -.
DR EnsemblBacteria; CAP03814; CAP03814; CTL0374.
DR KEGG; ctb:CTL0374; -.
DR PATRIC; fig|471472.4.peg.406; -.
DR HOGENOM; CLU_067042_0_0_0; -.
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 Coiled coil; Host membrane; Membrane; Secreted; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..273
FT /note="Inclusion membrane protein A"
FT /id="PRO_0000446189"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 206..233
FT /evidence="ECO:0000255"
FT CONFLICT 9
FT /note="T -> I (in Ref. 1; AAC82641)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 30260 MW; E0B3496A529B14EC CRC64;
MTTPTLIVTP PSPPAPSYSA NRVPQPSLMD KIKKIAAIAS LILIGTIGFL ALLGHLVGFL
IAPQITIVLL ALFITSLAGN ALYLQKTANL HLYQDLQREV GSLKEINFML SVLQKEFLHL
SKEFATTSKD LSAVSQDFYS CLQGFRDNYK GFESLLDEYK NSTEEMRKLF SQEIIADLKG
SVASLREEIR FLTPLAEEVR RLAHNQESLT AAIEELKTIR DSLRDEIGQL SQLSKTLTSQ
IALQRKESSD LCSQIRETLS SPRKSASPST KSS
