Y887_METMA
ID Y887_METMA Reviewed; 327 AA.
AC Q8PYH5;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Putative ABC transporter ATP-binding protein MM_0887;
DE EC=7.-.-.-;
GN OrderedLocusNames=MM_0887;
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; AAM30583.1; -; Genomic_DNA.
DR RefSeq; WP_011032837.1; NC_003901.1.
DR AlphaFoldDB; Q8PYH5; -.
DR SMR; Q8PYH5; -.
DR STRING; 192952.MM_0887; -.
DR EnsemblBacteria; AAM30583; AAM30583; MM_0887.
DR GeneID; 1479229; -.
DR KEGG; mma:MM_0887; -.
DR PATRIC; fig|192952.21.peg.1046; -.
DR eggNOG; arCOG00202; Archaea.
DR HOGENOM; CLU_000604_1_22_2; -.
DR OMA; RCIPFLE; -.
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:0006824; P:cobalt ion transport; IEA:InterPro.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 1.
DR Gene3D; 3.40.50.300; -; 1.
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; IPR005876; Co_trans_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01166; cbiO; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Reference proteome; Translocase; Transport.
FT CHAIN 1..327
FT /note="Putative ABC transporter ATP-binding protein
FT MM_0887"
FT /id="PRO_0000092147"
FT DOMAIN 47..282
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 81..88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 327 AA; 36074 MW; 6D4EF4727A3890E8 CRC64;
MSKSTPLKSS IIRADLPEQA EGRTGPETGK DPEKTGNSEG KTDTPVIEIK DLCHRYPHLE
ANALDRINLR IYRGERVAVL GANGAGKSTL FKHLNGILRP LSGEVLVKGE KITKKNVRMC
RGTVGIVFQD PDDQVLAPSV EEDVAFGPIN MGLSREEVKM RVKEALEMVG LNGFEERAPH
HLSGGQKKLV AIAGILAMRP EVIVLDEPTA GLDPLSSARV LKLITKMNRE LGITLLLSTH
DVDVVPYFAE RVFVLHHGKL EASGSPEEIF NDPALLRKAH LRLPRVAEVF EMLKQEGVDV
NIQITAETAR DEILRVIRSE NRKAEMK