ID   Y870_METAC              Reviewed;         641 AA.
AC   Q8TSC8;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Putative ABC transporter ATP-binding protein MA_0870;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=MA_0870;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(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; AE010299; AAM04309.1; -; Genomic_DNA.
DR   RefSeq; WP_011020914.1; NC_003552.1.
DR   AlphaFoldDB; Q8TSC8; -.
DR   SMR; Q8TSC8; -.
DR   STRING; 188937.MA_0870; -.
DR   EnsemblBacteria; AAM04309; AAM04309; MA_0870.
DR   GeneID; 1472762; -.
DR   KEGG; mac:MA_0870; -.
DR   HOGENOM; CLU_000604_86_7_2; -.
DR   InParanoid; Q8TSC8; -.
DR   OMA; MYRGEQV; -.
DR   OrthoDB; 25719at2157; -.
DR   PhylomeDB; Q8TSC8; -.
DR   Proteomes; UP000002487; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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..641
FT                   /note="Putative ABC transporter ATP-binding protein
FT                   MA_0870"
FT                   /id="PRO_0000092136"
FT   DOMAIN          10..250
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   DOMAIN          338..566
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   REGION          286..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..324
FT                   /note="Polar residues"
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         371..378
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   641 AA;  71163 MW;  007ACB2E778CB46A CRC64;
     MRKKEGRTMI EIKDLWYTYP GRTEPTLKGV NLKIEEGEFV LLTGPTGCGK STLLKTLNGI
     IPHESGGVFS GSIRVNGIET RNSNQMELSS AVGLVFQNPD DQIFSTSVED EVAFGPENLC
     LDREEIDKKV EEALRMVGMA EHRLDSTNAL SGGQKQRICI ASMLAMMPEI LAMDEPVSQM
     DPLGTREILN TVRELNRELK ITILLVEHRL HELMSFADRV VIMDGGKIVL DQPTSKAFDY
     IEVFHRLGLR VPEPVELCHT LGIKASPLSA EEALAVLGAG NCKEKVKTPR NFSNPEEETG
     RRTDPAERNE FVNTGSGNIK YGDNRSENKG SENRDSIISI RDLWSGYEKN RMVLKGINLE
     IRKGERVAIM GTNGSGKSTL LLNLAAMLKP YKGSVKVFGG DIQPRNSYSF AGRVGFVFQN
     PDLMLFCDSV DEEARFGPFQ LKYKDIEERT KTSLEAMSIL DLRQDLPQSL SRGQRLRTAV
     ASVLSIDPEI ILLDEPTTGQ DRVNIEHMMN YFKDNCSTLV FCTHDIEIAM LYATRLLVMD
     DGRIIADGKG REVIKNIEIL KQASLTQPPV VEIANYLGVD AISITELVEV LTRRSSEVKK
     DDGENYERMS SELTNSELAD SGVVNSELAD SGVVNSEGIK C