ID   CTRD_NEIMA              Reviewed;         216 AA.
AC   P57013; A1IP50;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Capsule polysaccharide export ATP-binding protein CtrD;
DE            EC=7.6.2.12;
DE   AltName: Full=Capsular-polysaccharide-transporting ATPase;
GN   Name=ctrD; OrderedLocusNames=NMA0195;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
CC   -!- FUNCTION: Putative ATP-binding protein, and an energy-coupling
CC       component of capsule polysaccharide export apparatus.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + capsular polysaccharide-[capsular polysaccharide-
CC         binding protein]Side 1 = ADP + phosphate + capsular
CC         polysaccharideSide 2 + [capsular polysaccharide-binding protein]Side
CC         1.; EC=7.6.2.12;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Peripheral
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; AL157959; CAM07509.1; -; Genomic_DNA.
DR   PIR; F82013; F82013.
DR   RefSeq; WP_002218516.1; NC_003116.1.
DR   AlphaFoldDB; P57013; -.
DR   SMR; P57013; -.
DR   PRIDE; P57013; -.
DR   EnsemblBacteria; CAM07509; CAM07509; NMA0195.
DR   KEGG; nma:NMA0195; -.
DR   HOGENOM; CLU_000604_1_2_4; -.
DR   OMA; VHIVYRV; -.
DR   BioCyc; NMEN122587:NMA_RS01005-MON; -.
DR   Proteomes; UP000000626; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015436; F:ABC-type capsular-polysaccharide transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd03220; ABC_KpsT_Wzt; 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; IPR015860; ABC_transpr_TagH-like.
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   3: Inferred from homology;
KW   ATP-binding; Capsule biogenesis/degradation; Cell inner membrane;
KW   Cell membrane; Membrane; Nucleotide-binding; Polysaccharide transport;
KW   Sugar transport; Translocase; Transport.
FT   CHAIN           1..216
FT                   /note="Capsule polysaccharide export ATP-binding protein
FT                   CtrD"
FT                   /id="PRO_0000092236"
FT   DOMAIN          2..215
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         38..45
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   216 AA;  24845 MW;  F265630711D674BF CRC64;
     MISVEHVSKR YLTRQGWRTV LHDISFKMEK GEKIGILGRN GAGKSTLIRL ISGVEPPTTG
     EIKRTMSISW PLAFSGAFQG SLTGMDNLRF ICRIYNVDID YVKNFTEEFS ELGQYLYEPV
     KRYSSGMKAR LAFALSLAVE FDCYLIDEVI AVGDSRFADK CKYELFEKRK DRSIILVSHS
     HSAMKQYCDN AMVLEKGHMY QFEDMDKAYE YYNSLP