CSEA_STRCO
ID CSEA_STRCO Reviewed; 225 AA.
AC Q9ZEP5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Lipoprotein CseA;
DE Flags: Precursor;
GN Name=cseA; OrderedLocusNames=SCO3357; ORFNames=SCE94.08;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / M600;
RX PubMed=10411727; DOI=10.1046/j.1365-2958.1999.01452.x;
RA Paget M.S.B., Leibowitz E., Buttner M.J.;
RT "A putative two-component signal transduction system regulates sigE, a
RT sigma factor required for normal cell wall integrity in Streptomyces
RT coelicolor A3(2).";
RL Mol. Microbiol. 33:97-107(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
RN [3]
RP DETERMINATION OF TRANSLATIONAL START SITE, SUBCELLULAR LOCATION,
RP CHARACTERIZATION, DIACYLGLYCEROL AT CYS-37, PALMITOYLATION AT CYS-37, AND
RP MUTAGENESIS OF CYS-37.
RC STRAIN=A3(2) / M600;
RX PubMed=17015661; DOI=10.1128/jb.00818-06;
RA Hutchings M.I., Hong H.J., Leibovitz E., Sutcliffe I.C., Buttner M.J.;
RT "The sigma(E) cell envelope stress response of Streptomyces coelicolor is
RT influenced by a novel lipoprotein, CseA.";
RL J. Bacteriol. 188:7222-7229(2006).
CC -!- FUNCTION: May be involved in the stabilization of the cell envelope or
CC may interact with the sensor protein CseC to modulate its activity, in
CC response to cell envelope stress.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17015661};
CC Lipid-anchor {ECO:0000269|PubMed:17015661}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA10324.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAB40857.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ131213; CAA10324.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL939116; CAB40857.1; ALT_INIT; Genomic_DNA.
DR PIR; T36368; T36368.
DR RefSeq; NP_627565.1; NC_003888.3.
DR AlphaFoldDB; Q9ZEP5; -.
DR STRING; 100226.SCO3357; -.
DR GeneID; 1098794; -.
DR KEGG; sco:SCO3357; -.
DR PATRIC; fig|100226.15.peg.3419; -.
DR eggNOG; ENOG502ZWYH; Bacteria.
DR HOGENOM; CLU_078792_0_0_11; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Cell membrane; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Signal.
FT SIGNAL 1..36
FT CHAIN 37..225
FT /note="Lipoprotein CseA"
FT /id="PRO_0000314479"
FT REGION 40..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 37
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:17015661"
FT LIPID 37
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000269|PubMed:17015661"
FT MUTAGEN 37
FT /note="C->A: Abolishes attachment to the membrane and
FT provokes rapid degradation of mutated protein."
FT /evidence="ECO:0000269|PubMed:17015661"
SQ SEQUENCE 225 AA; 23435 MW; AE78AE8D57AEE330 CRC64;
MRGLTDGRTP RGTRRTTQAA STAVAVFVAL GVSLAGCGTG GTGARDEGPA HADAVGGAGS
ASPAPAAKAS PSKAPDRVDA VRLVKADPKV SPEVKRELKP CVADEYPIDV SYGKVTDGSA
DDVVVNVLTC GDAVGVGSYV YREEDGAYQN VFKAEEPPVY AEIDRGDLVV TKQVYDKGDP
VSSPSGENVI TYRWASDRFT EEYRTHNDYS KAAGNAPTPA PEPDS