MOMPK_CHLPN
ID MOMPK_CHLPN Reviewed; 389 AA.
AC Q9XBF4; Q08085;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 2.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Major outer membrane porin;
DE Short=MOMP;
GN Name=ompA; Synonyms=omp1;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Koala type I;
RX PubMed=8125292; DOI=10.1016/0378-1119(94)90796-x;
RA Girjes A.A., Carrick F.N., Lavin M.F.;
RT "Remarkable sequence relatedness in the DNA encoding the major outer
RT membrane protein of Chlamydia psittaci (koala type I) and Chlamydia
RT pneumoniae.";
RL Gene 138:139-142(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 45-377.
RC STRAIN=Koala type I;
RX PubMed=8419295; DOI=10.1128/jb.175.2.487-502.1993;
RA Kaltenboeck B., Kousoulas K.G., Storz J.;
RT "Structures of and allelic diversity and relationships among the major
RT outer membrane protein (ompA) genes of the four chlamydial species.";
RL J. Bacteriol. 175:487-502(1993).
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 small cysteine-rich protein and the large cysteine-rich periplasmic
CC protein. It has been described in publications as the Sarkosyl-
CC insoluble COMC (Chlamydia outer membrane complex), and serves as the
CC functional equivalent of peptidoglycan (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Permits diffusion of specific solutes through the outer
CC membrane. {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).
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: It is present but some of the disulfide bonds are
CC reduced in reticulate bodies (RBs).
CC -!- SIMILARITY: Belongs to the chlamydial porin (CP) (TC 1.B.2) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally thought to originate from Chlamydia psittaci.
CC {ECO:0000305|PubMed:8125292}.
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DR EMBL; X72023; CAA50906.1; -; Genomic_DNA.
DR EMBL; M73038; AAD38210.1; -; Genomic_DNA.
DR PIR; I40864; I40864.
DR AlphaFoldDB; Q9XBF4; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR000604; Major_OMP_Chlamydia.
DR Pfam; PF01308; Chlam_OMP; 1.
DR PRINTS; PR01334; CHLAMIDIAOMP.
PE 2: Evidence at transcript level;
KW Cell outer membrane; Cell shape; Disulfide bond; Ion transport; Membrane;
KW Porin; Transmembrane; Transmembrane beta strand; Transport.
FT CHAIN 1..389
FT /note="Major outer membrane porin"
FT /id="PRO_0000207120"
FT CONFLICT 328
FT /note="A -> P (in Ref. 2; AAD38210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 41579 MW; 5DC50E85A6F4E50F CRC64;
MKKLLKSALL SAAFAGSVGS LQALPVGNPS DPSLLIDGTI WEGAAGDPCD PCATWCDAIS
LRAGFYGDYV FDRILKVDAP KTFSMGAKPT GSATANYTTA VDRPNPAYNK HLHDAEWFTN
AGFIALNIWD RFDVFCTLGA SNGYIKGNST AFNLVGLFGV KGTSVAANEL PNVSLSNGVV
ELYTDTSFSW SVGARGALWE CGCATLGAEF QYAQSKPKVE ELNVICNVAQ FSVNKPKGYK
GVAFPLPTDA GVATATGTKS ATINYHEWQV GASLSYRLNS LVPYIGVQWS RATFDADNIR
IAQPKLPTAV LNLTAWNPSL LGNTTTLATS DSFSDFMQIV SCQINKFKSR KACGVTVGAT
LVDADKWSLT AEARLINERA AHVSGQFRF