ID   MMDB_PROMO              Reviewed;         395 AA.
AC   O54031;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Methylmalonyl-CoA decarboxylase subunit beta {ECO:0000305};
DE            EC=7.2.4.3 {ECO:0000269|PubMed:9428714};
GN   Name=mmdB {ECO:0000303|PubMed:9428714};
OS   Propionigenium modestum.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Propionigenium.
OX   NCBI_TaxID=2333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP   AND SUBCELLULAR LOCATION.
RC   STRAIN=DSM 2376 / Gra Succ2;
RX   PubMed=9428714; DOI=10.1111/j.1432-1033.1997.0590a.x;
RA   Bott M., Pfister K., Burda P., Kalbermatter O., Woehlke G., Dimroth P.;
RT   "Methylmalonyl-CoA decarboxylase from Propionigenium modestum--cloning and
RT   sequencing of the structural genes and purification of the enzyme
RT   complex.";
RL   Eur. J. Biochem. 250:590-599(1997).
CC   -!- FUNCTION: Tunnel subunit of the sodium ion pump methylmalonyl-CoA
CC       decarboxylase, which converts the chemical energy of a decarboxylation
CC       reaction into an electrochemical gradient of Na(+) ions across the
CC       cytoplasmic membrane, thereby creating a sodium ion motive force that
CC       is used for ATP synthesis (PubMed:9428714). The beta subunit catalyzes
CC       the decarboxylation of the carboxybiotin carrier protein and the
CC       coupled export of Na(+) ions (By similarity).
CC       {ECO:0000250|UniProtKB:Q57286, ECO:0000269|PubMed:9428714}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-methylmalonyl-CoA + H(+)(out) + Na(+)(in) = CO2 +
CC         Na(+)(out) + propanoyl-CoA; Xref=Rhea:RHEA:21396, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:29101, ChEBI:CHEBI:57327,
CC         ChEBI:CHEBI:57392; EC=7.2.4.3; Evidence={ECO:0000269|PubMed:9428714};
CC   -!- SUBUNIT: The methylmalonyl-CoA decarboxylase is composed of four
CC       subunits: the carboxyltransferase alpha subunit (MmdA), the tunnel beta
CC       subunit (MmdB), the biotin-containing gamma subunit (MmdC) and the
CC       delta subunit (MmdD). {ECO:0000269|PubMed:9428714}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9428714};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:9428714}.
CC   -!- SIMILARITY: Belongs to the GcdB/MmdB/OadB family. {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; AJ002015; CAA05140.1; -; Genomic_DNA.
DR   PIR; T44985; T44985.
DR   SMR; O54031; -.
DR   KEGG; ag:CAA05140; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004492; F:methylmalonyl-CoA decarboxylase activity; IEA:RHEA.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR   InterPro; IPR005661; OadB_MmdB.
DR   PANTHER; PTHR35806; PTHR35806; 1.
DR   Pfam; PF03977; OAD_beta; 1.
DR   PIRSF; PIRSF015658; MmdB_OadB; 1.
DR   TIGRFAMs; TIGR01109; Na_pump_decarbB; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Ion transport; Membrane; Sodium; Sodium transport;
KW   Translocase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..395
FT                   /note="Methylmalonyl-CoA decarboxylase subunit beta"
FT                   /id="PRO_0000453536"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        128..148
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        230..250
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        304..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        374..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   395 AA;  41232 MW;  CFA30A8C17D3C69C CRC64;
     MLQAILDFYH STGFYGLNMG SIIMMLVACV FLYLAIAKEF EPLLLVPISF GILLTNLPFA
     GMMAEPLLEV HEKLSASGAH LYTAHTAEPG GLLYYLFQGD HLGIFPPLIF LGVGAMTDFG
     PLISNPKSLL LGAAAQFGIF VTFFGAIASG LFTAQEAASI GIIGGADGPT AIFLSSKLAP
     HLMGPIAVAA YSYMALVPII QPPIMTALTS ETERKIKMSQ LRLVSKREKI IFPIVVTILV
     SLIVPPAATL VGMLMLGNLF RECGVVGRLE DTAKNALINI ITIFLGVTVG ATATAEAFLK
     VETLAILGLG IVAFGIGTGS GVLLAKFMNK LSKEPINPLL GSAGVSAVPM AARVSQVVGQ
     KADPTNFLLM HAMGPNVAGV IGSAVSAGVL LSLFG