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Y1996_METMA
ID   Y1996_METMA             Reviewed;         581 AA.
AC   Q8PVG9;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Putative ABC transporter ATP-binding protein MM_1996;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=MM_1996;
OS   Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS   11833 / OCM 88) (Methanosarcina frisia).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=192952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX   PubMed=12125824;
RA   Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA   Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA   Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA   Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA   Fritz H.-J., Gottschalk G.;
RT   "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT   between Bacteria and Archaea.";
RL   J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
CC   -!- FUNCTION: Probably part of an ABC transporter complex. Responsible for
CC       energy coupling to the transport system (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AE008384; AAM31692.1; -; Genomic_DNA.
DR   RefSeq; WP_011033928.1; NC_003901.1.
DR   AlphaFoldDB; Q8PVG9; -.
DR   SMR; Q8PVG9; -.
DR   STRING; 192952.MM_1996; -.
DR   EnsemblBacteria; AAM31692; AAM31692; MM_1996.
DR   GeneID; 1480338; -.
DR   KEGG; mma:MM_1996; -.
DR   PATRIC; fig|192952.21.peg.2297; -.
DR   eggNOG; arCOG00188; Archaea.
DR   HOGENOM; CLU_000604_86_7_2; -.
DR   OMA; MYRGEQV; -.
DR   Proteomes; UP000000595; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Translocase; Transport.
FT   CHAIN           1..581
FT                   /note="Putative ABC transporter ATP-binding protein
FT                   MM_1996"
FT                   /id="PRO_0000092148"
FT   DOMAIN          10..250
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          313..541
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          287..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         44..51
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         346..353
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   581 AA;  64339 MW;  A48688AF22FA9E15 CRC64;
     MNQNRGSTII EIRDLWYTYP GRAETTLKGI DLKIKEGEFV LLTGPTGCGK STLLKTLNGI
     IPHESEGIFS GSIKISGIET VDSGQMELSK KAGLVFQSPD DQIFSTTVED EVAFGPENLC
     MEREEIDKKV DDALKMVGMS GHRLDSTNSL SGGQKQRVCI ASMLAMMPEI LAMDEPVSQM
     DPAGTQEILN TVRELNRKQN ITILLVEHRI HEIAPFADRV VIMDSGKIIL DQPASKAFEN
     LEVFHRLGLR VPEPVELCHT LGIKASPFSA EETFPLLNTG NFKEKIGDYP ASPGRKEKTS
     SPGWSSENNE PLVSVRDLWS GYDKSRMVLK GINLEIHRGE RVAVMGTNGS GKSTLLLNLA
     AMLRPYKGNV KIFGEDTKTK NPYSFAGRIG FVFQNPDLML FCDSTEEEAK FGPARLKLDN
     IEERAKISLE AMSILNLRKD LPQSLSRGQR LRTAVASILS IDPILVLLDE PTTGQDRVNI
     EQMMDYFKTR GSTLVFCTHD IEIAMLYATR ILVMNEGQII ADGRGRDVIK DIDILRKASL
     TQPPVVEIAS YLGIDAFSIT ELVDGLIHRN PEIRIAEGIK C
 
 
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