CTRD_NEIMB
ID CTRD_NEIMB Reviewed; 216 AA.
AC P32016;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 126.
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=NMB0074;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B1940 / Serogroup B;
RX PubMed=1659649; DOI=10.1111/j.1365-2958.1991.tb01899.x;
RA Frosch M., Edwards U., Bousset K., Krausse B., Weisgerber C.;
RT "Evidence for a common molecular origin of the capsule gene loci in Gram-
RT negative bacteria expressing group II capsular polysaccharides.";
RL Mol. Microbiol. 5:1251-1263(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(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; M57677; AAA25453.1; -; Genomic_DNA.
DR EMBL; AE002098; AAF40541.1; -; Genomic_DNA.
DR PIR; H81241; H81241.
DR PIR; S15223; S15223.
DR RefSeq; NP_273138.1; NC_003112.2.
DR RefSeq; WP_002224750.1; NC_003112.2.
DR AlphaFoldDB; P32016; -.
DR SMR; P32016; -.
DR STRING; 122586.NMB0074; -.
DR PaxDb; P32016; -.
DR EnsemblBacteria; AAF40541; AAF40541; NMB0074.
DR KEGG; nme:NMB0074; -.
DR PATRIC; fig|122586.8.peg.108; -.
DR HOGENOM; CLU_000604_1_2_4; -.
DR OMA; VHIVYRV; -.
DR Proteomes; UP000000425; 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 Reference proteome; Sugar transport; Translocase; Transport.
FT CHAIN 1..216
FT /note="Capsule polysaccharide export ATP-binding protein
FT CtrD"
FT /id="PRO_0000092237"
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"
FT CONFLICT 10..17
FT /note="RYLTRQGW -> QYQMRGGM (in Ref. 1; AAA25453)"
FT /evidence="ECO:0000305"
FT CONFLICT 22
FT /note="H -> D (in Ref. 1; AAA25453)"
FT /evidence="ECO:0000305"
FT CONFLICT 25..29
FT /note="SFKME -> NFSLQ (in Ref. 1; AAA25453)"
FT /evidence="ECO:0000305"
FT CONFLICT 34
FT /note="I -> V (in Ref. 1; AAA25453)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="I -> V (in Ref. 1; AAA25453)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="T -> S (in Ref. 1; AAA25453)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 216 AA; 24802 MW; 5608DEB1CABBC909 CRC64;
MISVEHVSKR YLTRQGWRTV LHDISFKMEK GEKIGILGRN GAGKSTLIRL ISGVEPPTTG
EIKRTMSISW PLAFSGAFQG SLTGMDNLRF ICRIYNVDID YVKAFTEEFS ELGQYLYEPV
KRYSSGMKAR LAFALSLAVE FDCYLIDEVI AVGDSRFADK CKYELFEKRK DRSIILVSHS
HSAMKQYCDN AMVLEKGHMY QFEDMDKAYE YYNSLP
