CPSC_STREE
ID CPSC_STREE Reviewed; 230 AA.
AC Q54519; O52233;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Capsular polysaccharide biosynthesis protein CpsC;
GN Name=cpsC; Synonyms=cps19fC;
OS Streptococcus pneumoniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Serotype 19F;
RX PubMed=7960118; DOI=10.1128/iai.62.12.5384-5396.1994;
RA Guidolin A., Morona J.K., Morona R., Hansman D., Paton J.C.;
RT "Nucleotide sequence analysis of genes essential for capsular
RT polysaccharide biosynthesis in Streptococcus pneumoniae type 19F.";
RL Infect. Immun. 62:5384-5396(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCTC 11906 / Serotype 19F, PO-329 / Serotype 19F,
RC SP-496 / Serotype 19F, SP-GA71 / Serotype 19F, SP-VA92 / Serotype 19F, and
RC SP-VA96 / Serotype 19F;
RX PubMed=9466257; DOI=10.1046/j.1365-2958.1998.00658.x;
RA Coffey T.J., Enright M.C., Daniels M., Morona J.K., Morona R.,
RA Hryniewicz W., Paton J.C., Spratt B.G.;
RT "Recombinational exchanges at the capsular polysaccharide biosynthetic
RT locus lead to frequent serotype changes among natural isolates of
RT Streptococcus pneumoniae.";
RL Mol. Microbiol. 27:73-83(1998).
RN [3]
RP FUNCTION.
RC STRAIN=Rx1-19F / Serotype 19F;
RX PubMed=10760144; DOI=10.1046/j.1365-2958.2000.01808.x;
RA Morona J.K., Paton J.C., Miller D.C., Morona R.;
RT "Tyrosine phosphorylation of CpsD negatively regulates capsular
RT polysaccharide biosynthesis in Streptococcus pneumoniae.";
RL Mol. Microbiol. 35:1431-1442(2000).
CC -!- FUNCTION: Required for CpsD phosphorylation. Involved in the regulation
CC of capsular polysaccharide biosynthesis. May be part of a complex that
CC directs the coordinated polymerization and export to the cell surface
CC of the capsular polysaccharide. {ECO:0000269|PubMed:10760144}.
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CpsC/CapA family. {ECO:0000305}.
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DR EMBL; U09239; AAC44960.1; -; Genomic_DNA.
DR EMBL; AF030367; AAC38718.1; -; Genomic_DNA.
DR EMBL; AF030368; AAC38723.1; -; Genomic_DNA.
DR EMBL; AF030369; AAC38728.1; -; Genomic_DNA.
DR EMBL; AF030370; AAC38732.1; -; Genomic_DNA.
DR EMBL; AF030371; AAC38737.1; -; Genomic_DNA.
DR EMBL; AF030372; AAC38742.1; -; Genomic_DNA.
DR RefSeq; WP_000664166.1; NZ_WNIA01000046.1.
DR RefSeq; WP_000664170.1; NZ_FYMI01000027.1.
DR AlphaFoldDB; Q54519; -.
DR SMR; Q54519; -.
DR OMA; NIQMANT; -.
DR UniPathway; UPA00934; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005351; F:carbohydrate:proton symporter activity; IEA:InterPro.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009103; P:lipopolysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0015774; P:polysaccharide transport; IEA:InterPro.
DR InterPro; IPR003856; LPS_length_determ_N_term.
DR InterPro; IPR005701; MPA1-like.
DR Pfam; PF02706; Wzz; 1.
DR TIGRFAMs; TIGR01006; polys_exp_MPA1; 1.
PE 3: Inferred from homology;
KW Capsule biogenesis/degradation; Cell membrane; Exopolysaccharide synthesis;
KW Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..230
FT /note="Capsular polysaccharide biosynthesis protein CpsC"
FT /id="PRO_0000217231"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VARIANT 60
FT /note="D -> N (in strain: NCTC 11906)"
FT VARIANT 216
FT /note="Q -> H (in strain: NCTC 11906)"
SQ SEQUENCE 230 AA; 25499 MW; F53E8A96135A2CFC CRC64;
MKEQNTLEID VLQLFRALWK RKLVILLVAI ITSSVAFAYS TFVIKPEFTS MTRIYVVNRD
QGEKSGLTNQ DLQAGSSLVK DYREIILSQD VLEEVVSDLK LDLTPKDLAN KIKVTVPVDT
RIVSVSVSDR VPEEASRIAN SLREVAAQKI ISITRVSDVT TLEEARPATS PSSPNIKRST
LIGFLAGVIG TSVIVLILEL LDTRVKRPKD IEDTLQMTLL GIVPNLNKLK
