ID   CTRC_NEIMA              Reviewed;         265 AA.
AC   P57012; A1IP51;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Capsule polysaccharide export inner-membrane protein CtrC;
GN   Name=ctrC; OrderedLocusNames=NMA0196;
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: May form an ATP-driven capsule polysaccharide export
CC       apparatus, in association with the CtrB and CtrD proteins.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC       {ECO:0000305}.
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DR   EMBL; AL157959; CAM07510.1; -; Genomic_DNA.
DR   PIR; G82013; G82013.
DR   RefSeq; WP_002236582.1; NC_003116.1.
DR   AlphaFoldDB; P57012; -.
DR   SMR; P57012; -.
DR   EnsemblBacteria; CAM07510; CAM07510; NMA0196.
DR   KEGG; nma:NMA0196; -.
DR   HOGENOM; CLU_060703_5_1_4; -.
DR   OMA; AFRQVQP; -.
DR   BioCyc; NMEN122587:NMA_RS01010-MON; -.
DR   Proteomes; UP000000626; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR013525; ABC_2_trans.
DR   InterPro; IPR000412; ABC_2_transport.
DR   Pfam; PF01061; ABC2_membrane; 1.
DR   PRINTS; PR00164; ABC2TRNSPORT.
DR   PROSITE; PS51012; ABC_TM2; 1.
PE   3: Inferred from homology;
KW   Capsule biogenesis/degradation; Cell inner membrane; Cell membrane;
KW   Membrane; Polysaccharide transport; Sugar transport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..265
FT                   /note="Capsule polysaccharide export inner-membrane protein
FT                   CtrC"
FT                   /id="PRO_0000182979"
FT   TRANSMEM        37..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..258
FT                   /note="ABC transmembrane type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00442"
SQ   SEQUENCE   265 AA;  30236 MW;  92E5AFCBCB20936E CRC64;
     MKELHKTSFL ESLLIQKRVI GALLMREIIT RYGRNNIGFL WLFVEPLLLT LVMVLMWKFF
     RMHNVSALNI VAFTLTGYPM MMMWRNASNH AIGSISANTS LLYHRNVRVL DTIFARMLLE
     IAGATIAQVV IMFALVIIGW IDVPADIFYM LLAWLLMAMF AVGLGLVICS VAFHFEPFGK
     VWSTISFVMM PLSGVFFFVH NLPQQLQHYV LMIPMVHGTE MFRAGYFGDS VTTYENPWYI
     LLCNLVLLLL GLAVVARFSK GVEPQ