ID   INCA_CHLCV              Reviewed;         355 AA.
AC   H2VFV1;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Inclusion membrane protein A {ECO:0000303|PubMed:15316015};
GN   Name=incA; OrderedLocusNames=CCA_00550;
OS   Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS   (Chlamydophila caviae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=227941;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX   PubMed=12682364; DOI=10.1093/nar/gkg321;
RA   Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA   Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA   Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA   Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA   Fraser C.M.;
RT   "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT   examining the role of niche-specific genes in the evolution of the
RT   Chlamydiaceae.";
RL   Nucleic Acids Res. 31:2134-2147(2003).
RN   [2]
RP   SUBUNIT, OLIGOMERIZATION, DOMAIN, AND MUTAGENESIS BY DOMAIN DELETION.
RC   STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
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 is probably involved in the homotypic fusion of
CC       inclusions. {ECO:0000250|UniProtKB:A0A0H3MD02}.
CC   -!- SUBUNIT: Forms homodimers, and probably higher-order oligomers too.
CC       {ECO:0000269|PubMed:15316015}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:A0A0H3MD02}. Host
CC       vacuole, host pathogen-containing vacuole, host pathogen-containing
CC       vacuole membrane {ECO:0000305|PubMed:15316015}; Multi-pass membrane
CC       protein {ECO:0000255}. Note=Secreted, probably by a type III secretion
CC       system (By similarity). Localized in the inclusion membrane (Probable).
CC       In the inclusion, the C-terminus faces the host cytosol (Probable).
CC       {ECO:0000250|UniProtKB:A0A0H3MD02, ECO:0000305|PubMed:15316015}.
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}.
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DR   EMBL; AE015925; AAP05293.1; -; Genomic_DNA.
DR   RefSeq; WP_011006508.1; NC_003361.3.
DR   AlphaFoldDB; H2VFV1; -.
DR   SMR; H2VFV1; -.
DR   EnsemblBacteria; AAP05293; AAP05293; CCA_00550.
DR   KEGG; cca:CCA_00550; -.
DR   HOGENOM; CLU_072760_0_0_0; -.
DR   OMA; QHETSLQ; -.
DR   OrthoDB; 1498440at2; -.
DR   Proteomes; UP000002193; 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; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Coiled coil; Host membrane; Membrane; Secreted; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..355
FT                   /note="Inclusion membrane protein A"
FT                   /id="PRO_0000446190"
FT   TRANSMEM        67..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        97..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..118
FT                   /note="Required for membrane anchoring"
FT                   /evidence="ECO:0000269|PubMed:15316015"
FT   REGION          320..355
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          243..298
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   355 AA;  38802 MW;  335AAD114D226351 CRC64;
     MTVSTDNTSP VISRASSPTF GDHGKDFDNN KIIPISIEAP TSSAAAVGAK TAIEPEGRSP
     LLQRICYLVK IIAAIALFVV GIAALVCLYL GSVISTPSLI LMLAIMLVSF VIVITAIRDG
     TPSQVVRHMK QQIQQFGEEN TRLHTAVENL KAVNVELSEQ INQLKQLHTR LSDFGDRLEA
     NTGDFTALIA DFQLSLEEFK SVGTKVETML SPFEKLAQSL KETFSQEAVQ AMMSSVTELR
     TNLNALKELI TENKTVIEQL KADAQLREEQ VRFLEKRKQE LEEACSTLSH SIATLQESTT
     LLKDSTTNLH AVESRLIGVM VQDGAESSTV EEASQDDSAQ PQDENQSDAG EHKDS