Y2387_METMA
ID Y2387_METMA Reviewed; 498 AA.
AC Q8PUE7;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Putative ABC transporter ATP-binding protein MM_2387;
DE EC=7.-.-.-;
GN OrderedLocusNames=MM_2387;
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; AAM32083.1; -; Genomic_DNA.
DR RefSeq; WP_011034311.1; NC_003901.1.
DR AlphaFoldDB; Q8PUE7; -.
DR SMR; Q8PUE7; -.
DR STRING; 192952.MM_2387; -.
DR EnsemblBacteria; AAM32083; AAM32083; MM_2387.
DR GeneID; 24879118; -.
DR KEGG; mma:MM_2387; -.
DR PATRIC; fig|192952.21.peg.2734; -.
DR eggNOG; arCOG00188; Archaea.
DR HOGENOM; CLU_000604_86_7_2; -.
DR OMA; YEACPND; -.
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..498
FT /note="Putative ABC transporter ATP-binding protein
FT MM_2387"
FT /id="PRO_0000092149"
FT DOMAIN 2..242
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 258..490
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 36..43
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 290..297
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 498 AA; 54819 MW; 81FF9A8792B1A02F CRC64;
MIELRNLSYT YGTAEEPSLK NINLKVKKGE LLLVTGHSAA GKTTLALAMA GILHHEIGGK
IEGNLSFKNR DIKEFDGIKE LSRHTGMVFD DAESQLIFTT VEEEILSGLE NRGYSGKEIQ
RRLNEVMELC EIGHLKERAP HTLSGGQKQK VALAATLALD TEVLILDEAT AELDTEAVRK
VFSVLKRLKE AEKTIIIVDH NIEDFLEIGD RVVLLEKGEI KAIKSPADFA AVSEDTDLTS
KSSKKEYSCS QKERQPVISI KNLTQRYGEF NALDNLDLEI RSGELVAILG ENGSGKTTLV
KHLNGLLRPY SGNVSVKGLN TSLTPVNELV KHTGLVFQNP DNMLFEDTVE AEVAFGLNNI
GITGSEAGDA IARSLELVNL KGKEKVFPRH LSRGERQRLA VACVIAMRPE LIILDEPTTG
LDAEESDRMM QLMKRLQLEG HTILMVTHNM QIVKDHAERV IRMASGKIVE DSANGACNSF
KRNIKCVEEK CAEGGAIV