1.B.64.1.1
Omp2a porin of 386 aas. The 3-d structure reveals a 16-stranded β-barrel with an α-helix on the third loop folding
inside the barrel and forming the constriction zone of the channel, a
typical feature of general porins (Lopes-Rodrigues et al. 2019). The preferential diffusion of cations over anions has been experimentally observed. Transports maltotetraose (Lopes-Rodrigues et al. 2019).
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| Accession Number: | Q44618 |
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| Protein Name: | Omp2a |
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| Length: | 386 |
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| Molecular Weight: | 40632.00 |
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| Species: | Brucella abortus [235] |
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| Number of TMSs: | 3 |
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| Location1 / Topology2 / Orientation3: |
Cell membrane1 / Peripheral membrane protein2 |
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| Substrate |
UDP-sugar, maltooligosaccharide |
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| Pfam: |
PF05244
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[1] “Species-specific sequences at the omp2 locus of Brucella type strains.” Ficht T.A. et.al. 8573514
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1: MLHEGNKKPG ISAGFLYPIR NGLERTLEAN DTAPSIVFSN GVLPLATKLG VGNFRRNGEA
61: RNQFVSNVSR NCRLAPVVMR SLQVEGSLLR SLILQTTPDS PIAAPLAVVL IRRSSGRICA
121: LQPNRELVGD VDVATNLGSP FFDDRVIGNN TSDRTPAASI LQAANNVRHV AVDVVVGRAS
181: VTTVVVATLF ESDHSREAVS ASEGVRDLAG AVGASRDHVI VDDIAEVTGE GMEFRFIDTN
241: AQTTELDIRE LHDGAAAGFI TIFTIYARIV RSIVEAQFGE GLEGAEFGFR TGGNAECETS
301: ALVPAIAVGT GVNVIAALYV VTDVTMDAQA GFGARNVEVA SAVSVANADI FNGFGLWRDD
361: CVGSLSAGSC NQSCSGAKEK ALDVHF