CTRA_NEIMA
ID CTRA_NEIMA Reviewed; 387 AA.
AC P32758; A1IP53;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Capsule polysaccharide export outer membrane protein CtrA;
DE Flags: Precursor;
GN Name=ctrA; OrderedLocusNames=NMA0198;
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 [GENOMIC DNA].
RC STRAIN=A1493 / Serogroup A;
RX PubMed=1371768; DOI=10.1128/iai.60.3.798-803.1992;
RA Frosch M., Mueller D., Bousset K., Mueller A.;
RT "Conserved outer membrane protein of Neisseria meningitidis involved in
RT capsule expression.";
RL Infect. Immun. 60:798-803(1992).
RN [2]
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: Involved in transport of capsular polysaccharides to the cell
CC surface. May function as a membrane anchor for capsular
CC polysaccharides. Possible porin properties.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the BexD/CtrA/VexA family. {ECO:0000305}.
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DR EMBL; M80593; AAA25457.1; -; Genomic_DNA.
DR EMBL; AL157959; CAM07512.1; -; Genomic_DNA.
DR PIR; A82014; A82014.
DR RefSeq; WP_002236580.1; NC_003116.1.
DR AlphaFoldDB; P32758; -.
DR SMR; P32758; -.
DR EnsemblBacteria; CAM07512; CAM07512; NMA0198.
DR KEGG; nma:NMA0198; -.
DR HOGENOM; CLU_038343_4_0_4; -.
DR OMA; DRADARN; -.
DR BioCyc; NMEN122587:NMA_RS01020-MON; -.
DR Proteomes; UP000000626; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015159; F:polysaccharide transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR003715; Poly_export.
DR Pfam; PF02563; Poly_export; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Capsule biogenesis/degradation; Cell outer membrane; Ion transport;
KW Lipoprotein; Membrane; Palmitate; Polysaccharide transport; Porin; Signal;
KW Sugar transport; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 19..387
FT /note="Capsule polysaccharide export outer membrane protein
FT CtrA"
FT /id="PRO_0000025217"
FT TOPO_DOM 19..29
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..39
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..53
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..63
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..79
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..89
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 90..113
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..123
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..131
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 132..141
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..154
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 155..157
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..167
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 168..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..184
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..387
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CONFLICT 317
FT /note="A -> R (in Ref. 1; AAA25457)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 41346 MW; 8E5F99209BE793DE CRC64;
MLKLKFCIVI SFLILGSACS AIPSSGPSAK KVVSLGQQSE AQIPEVELID VNHAVAQSLY
KAQVNQSFTQ FGDGYASTGT LNIGDVLDIM IWEAPPAVLF GGGLSSMGSG SAQQTKLPEQ
LVTARGTVSV PFVGDISVVG KTPGQVQEII KGRLKKMANQ PQVMVRLVQN NAANVSVIRA
GNSVRMPLTA AGERVLDAVA AVGGSTANVQ DTNVQLTRGN VVRTVALEDL VANPRQNILL
RRGDVVTMIT NPYTFTSMGA VGRTQEIGFS ARGLSLSEAI GRMGGLQDRR SDARGVFVFR
YTPLVELPAE RQDKWIAQGY GSEAEIPTVY RVNMADAHSL FSMQRFPVKN KDVLYVSNAP
LAEVQKFLSF VFSPVTSGAN SINNLTN
