CTRA_NEIMB
ID CTRA_NEIMB Reviewed; 391 AA.
AC P0A0V8; P32013;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Capsule polysaccharide export outer membrane protein CtrA;
DE Flags: Precursor;
GN Name=ctrA; OrderedLocusNames=NMB0071;
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 [GENOMIC DNA].
RC STRAIN=B1936 / Serogroup B;
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 [3]
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: 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; AE002098; AAF40538.1; -; Genomic_DNA.
DR PIR; S15220; S15220.
DR RefSeq; NP_273135.1; NC_003112.2.
DR RefSeq; WP_002215290.1; NC_003112.2.
DR AlphaFoldDB; P0A0V8; -.
DR SMR; P0A0V8; -.
DR STRING; 122586.NMB0071; -.
DR PaxDb; P0A0V8; -.
DR EnsemblBacteria; AAF40538; AAF40538; NMB0071.
DR GeneID; 61282337; -.
DR KEGG; nme:NMB0071; -.
DR PATRIC; fig|122586.8.peg.105; -.
DR HOGENOM; CLU_038343_4_0_4; -.
DR OMA; DRADARN; -.
DR Proteomes; UP000000425; 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;
KW Reference proteome; Signal; Sugar transport; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 23..391
FT /note="Capsule polysaccharide export outer membrane protein
FT CtrA"
FT /id="PRO_0000025218"
FT TOPO_DOM 23..33
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 34..43
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..57
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..67
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..83
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..93
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 94..117
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..127
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 128..135
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..145
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..148
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..158
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..161
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..171
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..178
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..188
FT /note="Beta stranded"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..391
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT LIPID 23
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 23
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ SEQUENCE 391 AA; 41949 MW; 0F9434CF247F9FAD CRC64;
MFKVKFYIRH AVLLLCGSLI VGCSAIPSSG PSAKKIVSLG QQSEVQIPEV ELIDVNHTVA
QLLYKAQINQ SFTQFGDGYA SAGTLNIGDV LDIMIWEAPP AVLFGGGLSS MGSGSAHQTK
LPEQLVTARG TVSVPFVGDI SVVGKTPGQV QEIIKGRLKK MANQPQVMVR LVQNNAANVS
VIRAGNSVRM PLTAAGERVL DAVAAVGGST ANVQDTNVQL TRGNVVRTVA LEDLVANPRQ
NILLRRGDVV TMITNPYTFT SMGAVGRTQE IGFSARGLSL SEAIGRMGGL QDRRSDARGV
FVFRYTPLVE LPAERQDKWI AQGYGSEAEI PTVYRVNMAD AHSLFSMQRF PVKNKDVLYV
SNAPLAEVQK FLSFVFSPVT SGANSINNLT N
