Y462_METMA
ID Y462_METMA Reviewed; 453 AA.
AC Q8PZN0;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putative ABC transporter ATP-binding protein MM_0462;
DE EC=7.-.-.-;
GN OrderedLocusNames=MM_0462;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM30158.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008384; AAM30158.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048045849.1; NC_003901.1.
DR AlphaFoldDB; Q8PZN0; -.
DR SMR; Q8PZN0; -.
DR STRING; 192952.MM_0462; -.
DR EnsemblBacteria; AAM30158; AAM30158; MM_0462.
DR GeneID; 1478804; -.
DR KEGG; mma:MM_0462; -.
DR PATRIC; fig|192952.21.peg.557; -.
DR eggNOG; arCOG00203; Archaea.
DR HOGENOM; CLU_000604_13_0_2; -.
DR OMA; ALCGKRC; -.
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..453
FT /note="Putative ABC transporter ATP-binding protein
FT MM_0462"
FT /id="PRO_0000092146"
FT DOMAIN 4..239
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 453 AA; 50024 MW; E028A6C7EB8C9263 CRC64;
MIILETRSLK YSYPDGTAAV QDINIEIKKG KKVAFVGQNG SGKSTLFLLL NGTLKPQEGE
ILFHGVPFKY DSKSLREIRK SVGIVFQNSD DQIFAPTVYQ DVAFGPANLG YSKERVDACV
QSALEYVGLI RLKDRPPHHL SGGQKKRVAI AGVMAMEPEV IILDEPLSNL DPVGADEIMD
LLNEFNHFGS TIIISTHDVD LAYRWSDYVF LMSNSKLIGQ GTPAEVFKEQ ELLKKVGLRQ
PTTLEIYHEI ERRGLAYGRN SPKTIPDLVN TLKPLDLMWV DVAPGVREGD NLNIGVMYGE
YATQSPYEAI NATVLHIHPN GRAIVELKRK GIKAGGVLLY DTDKYSPDEV RQIIKEGEIA
FVGAMGKKSK TLAEQDGIRL DVTSGVIDKS ILMALCGKRC LILTAGGMVD HALKRTREYV
DKSGIEFTVG VVNRDGGCKW LEETEGSPEK LKT