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}. 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; 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 //