1.B.2.1.2
Major outer membrance protein MomP (OmpA, Omp1, Omp1L2) of 394 aas; 1 N-terminal TMS Rodríguez-Marañón et al., 2002). This protein is covalently linked to two other cys-rich proteins via disulfide bonds, OmcA (Omp2A; Omp3) with 88 aas and 1 N-terminal TMS, and OmcB (Omp2, Omp2B) with 547 aas and 1 N-terminal TMS. Together these proteins comprise the Chlamydial outer membrane complex (COMC) (Findlay et al. 2005). MOMP is the most suitable substitute for whole cell targets for vaccine production, and
its delivery as a combined systemic and mucosal vaccine is most
effective (Phillips et al. 2019). It is also a drug target (Sadhasivam et al. 2019). The efficacy of a novel affitoxin targeting MOMP against Chlamydia trachomatis in vitro and in vivo has been reported (Li et al. 2024).
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| Accession Number: | P06597 |
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| Protein Name: | Major outer membrane porin |
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| Length: | 394 |
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| Molecular Weight: | 42550.00 |
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| Species: | Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B) [471472] |
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| Number of TMSs: | 1 |
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| Location1 / Topology2 / Orientation3: |
Cell outer membrane1 / Multi-pass membrane protein2 |
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| Substrate |
molecule |
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1: MKKLLKSVLV FAALSSASSL QALPVGNPAE PSLMIDGILW EGFGGDPCDP CTTWCDAISM
61: RMGYYGDFVF DRVLQTDVNK EFQMGAKPTT ATGNAAAPST CTARENPAYG RHMQDAEMFT
121: NAAYMALNIW DRFDVFCTLG ATSGYLKGNS ASFNLVGLFG DNENHATVSD SKLVPNMSLD
181: QSVVELYTDT TFAWSAGARA ALWECGCATL GASFQYAQSK PKVEELNVLC NAAEFTINKP
241: KGYVGQEFPL DLKAGTDGVT GTKDASIDYH EWQASLALSY RLNMFTPYIG VKWSRASFDA
301: DTIRIAQPKS ATTVFDVTTL NPTIAGAGDV KASAEGQLGD TMQIVSLQLN KMKSRKSCGI
361: AVGTTIVDAD KYAVTVETRL IDERAAHVNA QFRF