Y1934_STRMU
ID Y1934_STRMU Reviewed; 558 AA.
AC Q93D97; Q7CE91;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative ABC transporter ATP-binding protein SMU_1934c;
DE EC=7.-.-.-;
GN Name=sdcBA; OrderedLocusNames=SMU_1934c;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT11;
RX PubMed=12161466; DOI=10.1177/154405910208100715;
RA Tao L., Tanzer J.M.;
RT "Novel sucrose-dependent adhesion co-factors in Streptococcus mutans.";
RL J. Dent. Res. 81:505-510(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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; AF397166; AAL04084.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59544.1; -; Genomic_DNA.
DR RefSeq; NP_722238.1; NC_004350.2.
DR RefSeq; WP_002262130.1; NC_004350.2.
DR AlphaFoldDB; Q93D97; -.
DR SMR; Q93D97; -.
DR STRING; 210007.SMU_1934c; -.
DR EnsemblBacteria; AAN59544; AAN59544; SMU_1934c.
DR GeneID; 66818730; -.
DR KEGG; smu:SMU_1934c; -.
DR PATRIC; fig|210007.7.peg.1719; -.
DR eggNOG; COG1122; Bacteria.
DR HOGENOM; CLU_000604_86_7_9; -.
DR OMA; DPMTRLD; -.
DR PhylomeDB; Q93D97; -.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR CDD; cd03225; ABC_cobalt_CbiO_domain1; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR022216; ABC_Co_transporter.
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 Pfam; PF12558; DUF3744; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
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..558
FT /note="Putative ABC transporter ATP-binding protein
FT SMU_1934c"
FT /id="PRO_0000092097"
FT DOMAIN 5..246
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 295..527
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 328..335
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 558 AA; 62386 MW; 43EA4D2AE1FD0F0F CRC64;
MKPFIEFKDF SFKYDAQAEP TLKEITLSIE KGEKVLIIGP SGSGKSTIGH CLNGIIPNIY
KGQAEGSLTI DGKDVFDLSI YEKSHLVSTV LQDPDGQFIG LTVAEDLAFA LENDCVAHET
MFERVDTWAD KLDLKELLQH RPQDLSGGQK QRVSLAGVMI DESPVLLFDE PLANLDPKSG
QDTIDLIDHL HQTAETTTII IEHRLEDVLY RPVDRVILIN EGQVLFNGSP NDLLKTSLLQ
ENGIREPLYV TVLRHLGLDI KNTSHLANLE QLDLSGVSFA GDISLKEPQE PQVLFDIQHL
NFAYSSERPI LKNLSFTLNK GERLAIVGKN GAGKSTLAKA LCQFISYAGQ IFYQGQDIAS
DSIKERSERI GYVLQNPNQM ISQTMIFDEV ALGLRLRGVD DSQIEKRVLK VLKTCGLYEF
RKWPISALSF GQKKRVTIAS ILVLNPEVIL LDEPTAGQDK KHYTEMMSFL NDLHALGHTI
IMITHDMQLM LEYSDRALVI SDGQILADQS PITLFNQPDI LRIANLKQTS IFDLAQRLNC
DPIALTHYYI DQQGGEDE