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. 2003 Jan;185(2):674–678. doi: 10.1128/JB.185.2.674-678.2003

TABLE 1.

Partial protein sequence alignment of the membrane fragments of c subunits (AtpE) of F1F0-type ATPases and K subunits (NtpK) of the A/V-type ATPases

Enzyme Organism or sourcea Sequenceb Total length (amino acids) of protein
F1F0-type H+ ATPase E. coli 19LAAIGAAIGIGILGG-19-FFIVMGLVDAIPMIAVGL70 79
V. cholerae 18LCAVGTAIGFAVLGG-19-MFIIAGLLDAVPMIGIVI69 85
V. alginolyticus 18LASLGTAIGFALLGG-19-MFIIAGLLDAVPMIGIVI69 84
B. subtilis 12LGALGAGIGNGLIVS-19-MFMGIALVEALPIIAVVI63 70
E. hirae 12GAAIGAGYGNGQVIS-19-MFIGVALVEAVPILGVVI63 71
Yeast mitochondria 17IGLLGAGIGIAIVFA-19-AILGFALSEATGLFCLMV68 74
Human mitochondria 82VGVAGSGAGIGTVFG-19-AILGFALSEAMGLFCLMV143 136
F1F0-type Na+ ATPase A. woodii c3 20IAGVGPGIGQGFAAG-19-MLLGAAVAETTGIYGLIV71 82
A. woodii c1 44VAGVGPGIGQGFAAG-19-MLLGAAVAETSGIFSLVI88 182
120IAGIGPGTGQGYAAG-19-MLLGQAVAQTTGIYALIV171 182
P. modestum 23IAGIGPGVGQGYAAG-19-MVLGQAIAESTGIYSLVI74 89
T. maritima 26IGAIGPGIGEGNIGA-19-MLLADAVAETTGIYSLLI77 85
F1F0-type ATPase unknown cation Mycoplasma genitalium 41IAGSTVGIGQGYIFG-19-IFIGSAVSESTAIYGLLI92 102
Mycoplasma pneumoniae 44VGGATVGLGQGYIFG-19-IFIGSAISESSSIYSLLI95 105
U. urealyticum 50LAAGAVGLMQGFSTA-19-MIVGLALAEAVAIYALIV81 89
S. pyogenes 9LACFGVSLAEGFLMA-19-MILGVAFIEGTFFVTLVM60 65
A/V-type H+ ATPase Halobacterium salinarum 16LAALAAGYAERGIGS-15-GLILTVLPETLVILALVV63 71
Sulfolobus acidocaldarius 45LAAIGAGVAVGMAAA-15-ILIFVAIGEGIAVYGILF92 101
Yeast VMA11 30LSCLGAAIGTAKSGI-15-SLIPVVMSGILAIYGLVV76 164
107FACLSSGYAIGMVGD-15-IVLILIFSEVLGLYGMIV154 164
A/V-type Na+ ATPase E. hirae 24FSGIGSAKGVGMTGE-15-ALILQLLPGTQGLYGFVI72 156
101FTGLFSGIAQGKVAA-15-GIIFAAMVETYAILGFVI148 156
C. trachomatis 14LAMIGSAVGCGMAGV-15-IIGLSAMPSSQSIYGLIF62 141
89SALLLSAFMQGKCCV-15-SFASIGIVESFALFAFVF136 141
S. pyogenes 26LSGMGSAYGVGKGGQ-15-ALILQLLPGSQGIYGFAI74 159
103IVGYFSAKHQGNVSV-15-GVILAAMVETYAILAFVV150 159
T. pallidum 14ISAVGSALGLALAGQ-19-LLAFAGAPLTQTIYGFLL65 140
88LGIAASALSQGRAAA-15-YLTIVGLCETVALLVMVF135 140
a

The organisms, sequence accession numbers in the NCBI protein database, and the references for experimentally studied proteins are as follows: E. coli P00844 (26), V. cholerae AAF95908, V. alginolyticus P12991 (23), B. subtilis P37815 (31), E. hirae P26682 (33) and BAA04271 (21), yeast mitochondria P00841 (25), human mitochondria P05496 (7), A. woodii AAF01475 (27) and AAF01474 (28), P. modestum CAA46895 (20), T. maritima AAD36682, M. genitalium P47644, M. pneumoniae AAC43654, U. urealyticum AAF30542, S. pyogenes AAK33697 (AtpE) and AAK33254 (NtpK), H. salinarium BAA13179 (18), S. acidocaldarius AAA72703 (4), yeast vacuole P32842 (35), C. trachomatis AAC67897, and T. pallidum AAC65416.

b

Residues involved in cation binding are underlined. The Gly23 and Gly27 residues, creating the cavity for Asp61 in the E. coli enzyme (11), are shown in boldface type.