5.B.5.1.3 Extracellular respiratory system with 3 cytochrome protein components, a periplasmic protein, MtrD, of 321 aas, a porin-type protein, MtrE, of 712 aas, and a surface decaheme cytochrome c component, MtrF, of 639 aas. Each protein has a single N-terminal targeting TMS. They function together in the reduction of extracellular iron and manganese oxides (Barrozo et al. 2018) using a cytoplasmic electron donor. These 3 proteins are parologous to MtrABC (TC# 5.B.5.1.1) and function in parallel, except that in contrast to MtrABC, no increase in mtrDEF gene expression is observed under O2‐limited conditions (Barchinger et al. 2016). This process is being exploited for the generation of renewable
energy technologies incorporating microbial catalysts on electrode
surfaces for fuel‐to‐electricity (microbial fuel cells) or
electricity‐to‐fuel (microbial electrosynthesis) conversion (Rabaey and Rozendal 2010; Santoro et al. 2017).
|
Accession Number: | Q8EG31 |
Protein Name: | Extracellular respiratory sytem outer membrane component MtrE |
Length: | 712 |
Molecular Weight: | 79186.00 |
Species: | Shewanella oneidensis (strain MR-1) [211586] |
Number of TMSs: | 1 |
Substrate |
electron |
---|
1: MQIVNISTPK VCFSLTLLAW TMSGVLNTAH AEGYEIQKAN RSGVKNEAWS CKQCQPQTGR
61: QGNVSATLAH NDGDDSRFGN RTGIDKDGLV GAIGADMKYK AESGYQTSLM ADKLGFDTGS
121: AKLSTGQLGH YQINLGYKGL ANYQYNQLKS PYIAENDKML LPDNWVAGAT TQSMPLLQSS
181: LAEQDLSLKR DRFNLGGYYA GHISSTNRYK ASINYQHENR SGAKKTSANI LTNSVMLAQP
241: IDDSTDEIDA RIYFGGIGWQ AGINSQISQY KNDHQALLWQ SAYTPTFGAA YYGQNAVEPD
301: NKAYRIAAEA SGGQNGHNVL MHAGISQMSQ DEAFLPATIN GPAPTLPADN LDGQVDILEM
361: LLKYSGRITQ DLSIQANYHY QDKDNKTTQL DFPQVVTDSV YQGTAQNSLY DKRSNKLELK
421: GKYRLTPSAY AEAGYSLDAN DYSALDRQSV DESGVFAKLS YRYSPSWSTW LKGEALTRDG
481: SEYDPVSTTQ SPSNPWLRKS YLADRKRQKV TLHTDYQSDI GLSVGASLHN VDDDYNHTSV
541: GLTHVSYLGY DVSAQYLIAD NLSLNAYLNQ DWRDSDQAGS NRFSTPDWYS TAEEKSTLIG
601: TGVVYQNLLD NHLDLGLDYS YSDGQSDTEV TYGITSPYGD YYNRKHNINA YAKYKLADSM
661: SLRFDWLFEK YQDASWQNQN TTWDTIPNVL SFGDISRDYN AHYLGLTLSY QM