ID   MTSC_STRGN              Reviewed;         251 AA.
AC   P42360;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Manganese import ATP-binding protein ScaC {ECO:0000305};
DE            EC=7.2.2.5 {ECO:0000269|PubMed:9440518};
DE   AltName: Full=ORF1 {ECO:0000303|PubMed:7927711};
GN   Name=scaC {ECO:0000303|PubMed:9440518};
OS   Streptococcus gordonii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1302;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 51656 / PK488;
RX   PubMed=7927711; DOI=10.1128/iai.62.10.4469-4480.1994;
RA   Kolenbrander P.E., Andersen R.N., Ganeshkumar N.;
RT   "Nucleotide sequence of the Streptococcus gordonii PK488 coaggregation
RT   adhesin gene, scaA, and ATP-binding cassette.";
RL   Infect. Immun. 62:4469-4480(1994).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 51656 / PK488, and
RC   Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288;
RX   PubMed=9440518; DOI=10.1128/jb.180.2.290-295.1998;
RA   Kolenbrander P.E., Andersen R.N., Baker R.A., Jenkinson H.F.;
RT   "The adhesion-associated sca operon in Streptococcus gordonii encodes an
RT   inducible high-affinity ABC transporter for Mn2+ uptake.";
RL   J. Bacteriol. 180:290-295(1998).
CC   -!- FUNCTION: Part of the high-affinity ABC transporter complex ScaABC
CC       involved in manganese import. Probably responsible for energy coupling
CC       to the transport system. Essential for growth under Mn(2+)-limiting
CC       conditions. {ECO:0000269|PubMed:9440518}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + Mn(2+)(out) = ADP + H(+) + Mn(2+)(in) + phosphate;
CC         Xref=Rhea:RHEA:17365, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29035, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=7.2.2.5;
CC         Evidence={ECO:0000269|PubMed:9440518};
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (ScaC),
CC       two transmembrane proteins (ScaB) and a solute-binding protein (ScaA).
CC       {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane
CC       protein {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Inactivation of the gene results in both impaired
CC       growth and strong inhibition of Mn(2+) uptake.
CC       {ECO:0000269|PubMed:9440518}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; L11577; AAA71945.1; -; Genomic_DNA.
DR   PIR; T11549; T11549.
DR   AlphaFoldDB; P42360; -.
DR   SMR; P42360; -.
DR   TCDB; 3.A.1.15.2; the atp-binding cassette (abc) superfamily.
DR   PRIDE; P42360; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015410; F:ABC-type manganese transporter activity; IDA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Manganese; Membrane; Nucleotide-binding;
KW   Translocase; Transport.
FT   CHAIN           1..251
FT                   /note="Manganese import ATP-binding protein ScaC"
FT                   /id="PRO_0000093283"
FT   DOMAIN          14..245
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         46..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   251 AA;  28055 MW;  AED59C66F677D031 CRC64;
     MLRYINTVGV IYMIEIQNLS VSYQGQLALD KANVTIKGPT ITGIIGPNGA GKSTLIKGLL
     GIVDHQGQAL LDGQPLDKEL KRIAYVEQKI NIDYNFPIKV KECVSLGLYP KIKLFQRLKT
     SDWDKVNQAL KIVGLEDFAE RQISQLSGGQ FQRVLIARCL VQEADYIFLD EPFVGIDSVS
     EEIIMKTLRQ LRKDGKTILI VHHDLSKVVA YFDQVLLLNK KVVAFGSTES TFTKENMQQT
     YGSQLFMNGG A