1.B.6.1.4
HMP-AB outer membrane porin, OmpAb or Omp38 (Gribun et al., 2004). It is the principle porin with an inner diameter of 2 nm which allows transport of cephalothin, cephaloridine, other antibiotics as well as other small molecules across the outer membrane (Sugawara and Nikaido 2012). Structural studies have been reported (Vashist and Rajeswari 2006). It is a secreted emulifier in some strains of Acinetobacter (Walzer et al. 2006). The sequence provided may be slightly incorrect (see the Q6BYW5 sequence of 356 aas).
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| Accession Number: | Q8KWW6 |
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| Protein Name: | HMP-AB outer membrane porin |
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| Length: | 346 |
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| Molecular Weight: | 37817.00 |
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| Species: | Acinetobacter baumannii [470] |
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| Number of TMSs: | 1 |
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| Location1 / Topology2 / Orientation3: |
Cell membrane1 / Multi-pass membrane protein2 |
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| Substrate |
molecule, antimicrobial agent, cefaloridine |
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1: MKLSRIALAT MLVAAPLAAA NAGVTVTPLL LGYTFQDTQH NNGGKDGELT NGPELQDDLF
61: VGAALGIELT PWLGFEAEYN QVKGDVDGLA AGAEYKQKQI NGNFYVTSDL ITKNYDSKIK
121: PYVLLGAGHY KYEIPDLSYH NDEEGTLGNA GVGAFWRLND ALSLRTEARG NLYFDEKFWN
181: YTALAGLNVV LGGHLKPAAP VVEVAPVEPT PVAPQPQELT EDLNMELRVF FDTNKSNIKD
241: QYKPEIAKVA EKLSEYPNAT ARIEGHTDNT GPRKLNERLS LARANSVKSA LVNEYNVDAS
301: RLSTQGFAWD QPIADNKTKE GRAMNRRVFA TITGSRTVLA EQPVAQ