P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334218    1 VVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 62
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334218    1 VVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 62
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334218      2 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 62
Cdd:TIGR02203 508 VQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334218    1 VVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 62
Cdd:cd03249 177 LVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1334218    2 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQAGAKRS 68
Cdd:COG5265 533 IQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 1334218    2 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKG 53
Cdd:cd03254 178 IQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334218    2 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQA 63
Cdd:COG2274 650 ILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711

lipid A ABC transporter ATP-binding protein/permease MsbA;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1334218     2 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQAG 64
Cdd:PRK11176 519 IQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1334218      2 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 62
Cdd:TIGR02204 515 VQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1334218      7 DKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMV 59
Cdd:TIGR00958 659 SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1334218    1 VVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQ 62
Cdd:cd03252 176 AIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

                        10        20        30
                ....*....|....*....|....*....|....*..
gi 1334218    2 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQ 38
Cdd:cd03228 135 ILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 1334218     2 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSM 58
Cdd:PRK11174 524 VMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1334218     13 RTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSV 61
Cdd:TIGR01193 660 KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]

                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1334218       1 VVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSM 58
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516

multidrug resistance protein (mdr1); Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1334218      8 KAREGRTCIVIAHRLSTIQNADLIVVIQNGQ-----VKEHGTHQQLL-AQKGIY 55
Cdd:PTZ00265 1405 KDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLsVQDGVY 1458

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334218    1 VVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQK-GIYFSMV 59
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253

ABC transporter; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1334218     14 TCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQL-LAQKGIYFSMV 59
Cdd:PTZ00243 1497 TVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD

                          10        20        30
                  ....*....|....*....|....*....|....
gi 1334218      1 VVQEALDKAREGRTCIVIAHRLSTIQNADLIVVI 34
Cdd:TIGR02857 496 EVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529

multidrug resistance protein (mdr1); Provisional

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1334218      1 VVQEALD--KAREGRTCIVIAHRLSTIQNADLIVVIQNGQ---------------------------------------- 38
Cdd:PTZ00265  617 LVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiigedptkdnkennnknnkddnnnnnnnnnnk 696

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1334218     39 -------VKEHGTHQQLLAQK-GIYFSMVSVQ 62
Cdd:PTZ00265  697 innagsyIIEQGTHDALMKNKnGIYYTMINNQ 728

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.

                        10        20
                ....*....|....*....|....*....
gi 1334218   10 REGRTCIVIAHRLSTIQNADLIVVIQNGQ 38
Cdd:cd03250 176 LNNKTRILVTHQLQLLPHADQIVVLDNGR 204

cobalt transporter ATP-binding subunit; Provisional

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 1334218     1 VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQLLAQKGIY 55
Cdd:PRK13631 215 MMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 1334218    8 KAREGRTCIVIAHRLSTI-QNADLIVVIQNGQVKEHGTHQQLLAQ 51
Cdd:COG1123 189 QRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233