ID   OMCA_CHLPS              Reviewed;          87 AA.
AC   P0CZ19; P27606;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 21.
DE   RecName: Full=Small cysteine-rich outer membrane protein omcA;
DE            Short=Small-CRP;
DE   AltName: Full=9 kDa cysteine-rich lipoprotein;
DE            Short=9KD-CRP;
DE   Flags: Precursor;
GN   Name=omcA; Synonyms=envA;
OS   Chlamydia psittaci (Chlamydophila psittaci).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83554;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DEVELOPMENTAL STAGE.
RC   STRAIN=A22/M;
RX   PubMed=7582008; DOI=10.1099/13500872-141-10-2489;
RA   Watson M.W., Clarke I.N., Everson J.S., Lambden P.R.;
RT   "The CrP operon of Chlamydia psittaci and Chlamydia pneumoniae.";
RL   Microbiology 141:2489-2497(1995).
CC   -!- FUNCTION: In elementary bodies (EBs, the infectious stage, which is
CC       able to survive outside the host cell) provides the structural
CC       integrity of the outer envelope through disulfide cross-links with the
CC       large cysteine-rich periplasmic protein and the major outer membrane
CC       porin. It has been described in publications as the Sarkosyl-insoluble
CC       COMC (Chlamydia outer membrane complex), and serves as the functional
CC       equivalent of peptidoglycan (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Part of a disulfide cross-linked outer membrane complex (COMC)
CC       composed of the major outer membrane porin (MOMP), the small cysteine-
CC       rich protein (omcA) and the large cysteine-rich periplasmic protein
CC       (omcB). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}. Note=The protein moiety probably penetrates into the
CC       periplasm.
CC   -!- DEVELOPMENTAL STAGE: It is present but the disulfide bonds are reduced
CC       in the intracellular reticulate bodies (RBs).
CC       {ECO:0000269|PubMed:7582008}.
CC   -!- PTM: N-terminal amide-linked and S-diacylglycerol cysteine-linked to
CC       16:0, 18:0, 15:0 branched, and 17:0 branched fatty acids (ratio
CC       6:5:3:4) in the EB stage. The exact distribution of fatty acids has not
CC       been determined (By similarity). {ECO:0000250}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000250}.
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; X53512; CAA37591.1; -; Genomic_DNA.
DR   RefSeq; WP_006342860.1; NZ_PJPZ01000001.1.
DR   AlphaFoldDB; P0CZ19; -.
DR   GeneID; 12242468; -.
DR   OMA; PDGRCKQ; -.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:InterPro.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   InterPro; IPR003517; Cys-rich_OMP3_Chlamydia.
DR   Pfam; PF03503; Chlam_OMP3; 1.
DR   PRINTS; PR01335; CHLAMIDIAOM3.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   2: Evidence at transcript level;
KW   Cell outer membrane; Cell shape; Disulfide bond; Lipoprotein; Membrane;
KW   Palmitate; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           20..87
FT                   /note="Small cysteine-rich outer membrane protein omcA"
FT                   /id="PRO_0000018157"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   87 AA;  8981 MW;  EA27764B791E8180 CRC64;
     MKKAVLLATV FCGVVGLTSC CRIVDCCFED PCAPKPCNPC GNKKDKGCSP CGVYTPSCSK
     PCGSECNPGV QGPQAKGCTS LDGRCKQ