MOMP_CHLT2
ID MOMP_CHLT2 Reviewed; 394 AA.
AC P06597; B0B8Q7; Q20KU8;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Major outer membrane porin;
DE Short=MOMP;
DE Flags: Precursor;
GN Name=ompA; Synonyms=omp1L2; OrderedLocusNames=CTL0050;
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].
RX PubMed=2946665; DOI=10.1128/jb.168.3.1277-1282.1986;
RA Stephens R.S., Mullenbach G., Sanchez-Pescador R., Agabian N.;
RT "Sequence analysis of the major outer membrane protein gene from Chlamydia
RT trachomatis serovar L2.";
RL J. Bacteriol. 168:1277-1282(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16369014; DOI=10.1128/iai.74.1.578-585.2006;
RA Brunelle B.W., Sensabaugh G.F.;
RT "The ompA gene in Chlamydia trachomatis differs in phylogeny and rate of
RT evolution from other regions of the genome.";
RL Infect. Immun. 74:578-585(2006).
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 PROTEIN SEQUENCE OF 23-27.
RA Bini L., Santucci A., Magi B., Marzocchi B., Sanchez-Campillo M.,
RA Comanducci M., Christianen G., Birkelund S., Vtretou E., Ratti G.,
RA Pallini V.;
RL Submitted (SEP-1994) to UniProtKB.
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}.
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DR EMBL; M14738; AAA23151.1; -; Genomic_DNA.
DR EMBL; DQ064295; ABB51013.1; -; Genomic_DNA.
DR EMBL; AM884176; CAP03494.1; -; Genomic_DNA.
DR PIR; S11012; S11012.
DR RefSeq; WP_009873292.1; NC_010287.1.
DR RefSeq; YP_001654141.1; NC_010287.1.
DR AlphaFoldDB; P06597; -.
DR TCDB; 1.B.2.1.2; the chlamydial porin (cp) family.
DR EnsemblBacteria; CAP03494; CAP03494; CTL0050.
DR KEGG; ctb:CTL0050; -.
DR PATRIC; fig|471472.4.peg.54; -.
DR HOGENOM; CLU_693881_0_0_0; -.
DR OMA; SGDPCDP; -.
DR Proteomes; UP000000795; Chromosome.
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 1: Evidence at protein level;
KW Cell outer membrane; Cell shape; Direct protein sequencing; Disulfide bond;
KW Ion transport; Membrane; Porin; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 23..394
FT /note="Major outer membrane porin"
FT /id="PRO_0000020152"
SQ SEQUENCE 394 AA; 42550 MW; BB5B7B80EB289CA5 CRC64;
MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISM
RMGYYGDFVF DRVLQTDVNK EFQMGAKPTT ATGNAAAPST CTARENPAYG RHMQDAEMFT
NAAYMALNIW DRFDVFCTLG ATSGYLKGNS ASFNLVGLFG DNENHATVSD SKLVPNMSLD
QSVVELYTDT TFAWSAGARA ALWECGCATL GASFQYAQSK PKVEELNVLC NAAEFTINKP
KGYVGQEFPL DLKAGTDGVT GTKDASIDYH EWQASLALSY RLNMFTPYIG VKWSRASFDA
DTIRIAQPKS ATTVFDVTTL NPTIAGAGDV KASAEGQLGD TMQIVSLQLN KMKSRKSCGI
AVGTTIVDAD KYAVTVETRL IDERAAHVNA QFRF