ID   CSP1_CORGL              Reviewed;         657 AA.
AC   P0C1D6; Q01377;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Protein PS1;
DE   Flags: Precursor;
GN   Name=csp1; Synonyms=cop1; OrderedLocusNames=Cgl2875, cg3182;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
CC   -!- FUNCTION: One of the two major secreted proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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DR   EMBL; BA000036; BAC00269.1; -; Genomic_DNA.
DR   EMBL; BX927156; CAF20900.1; -; Genomic_DNA.
DR   RefSeq; NP_602067.1; NC_003450.3.
DR   RefSeq; WP_011015455.1; NC_003450.3.
DR   PDB; 6SWZ; X-ray; 2.00 A; AAA=412-657.
DR   PDB; 6SX4; X-ray; 2.80 A; AAA/BBB/CCC/DDD=44-657.
DR   PDBsum; 6SWZ; -.
DR   PDBsum; 6SX4; -.
DR   AlphaFoldDB; P0C1D6; -.
DR   SMR; P0C1D6; -.
DR   STRING; 196627.cg3182; -.
DR   ESTHER; corgl-csp1; A85-Mycolyl-transferase.
DR   KEGG; cgb:cg3182; -.
DR   KEGG; cgl:Cgl2875; -.
DR   PATRIC; fig|196627.13.peg.2807; -.
DR   eggNOG; COG0627; Bacteria.
DR   eggNOG; COG5479; Bacteria.
DR   HOGENOM; CLU_026624_3_3_11; -.
DR   OMA; SGTHSWP; -.
DR   Proteomes; UP000000582; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000801; Esterase-like.
DR   InterPro; IPR013207; LGFP.
DR   Pfam; PF00756; Esterase; 1.
DR   Pfam; PF08310; LGFP; 4.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..43
FT                   /evidence="ECO:0000250"
FT   CHAIN           44..657
FT                   /note="Protein PS1"
FT                   /id="PRO_0000021028"
FT   CONFLICT        54
FT                   /note="I -> V (in Ref. 2; CAF20900)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   657 AA;  70674 MW;  E2C3F1B57A7938A3 CRC64;
     MRDTAFRSIK AKAQAKRRSL WIAAGAVPTA IALTMSLAPM ASAQSSNLSS DAVIGSIAQG
     VTDGLTDYLK PRVEELPAGE VTYPEIAGLP DGVRVISAEW ATSKHVILTI QSAAMPERPI
     KVQLLLPRDW YSSPNREFPE IWALDGLRAI EEQSGWTIET NIEQYYADKN AIVVLPVGGE
     SSFYSDWEGP NNGKNYQWET FLTQELAPIL DKGFRSNTDR AITGISMGGT AAVNIATHHP
     DMFKFVGSFS GYLDTTSAGM PIAISAALAD AGGYDANAMW GPVGSERWQE NDPKSNVDKL
     KGKTIYVSSG NGADDFGKEG SVAIGPANAA GVGLEVISRM TSQTFVDRAS QAGVEVVASF
     RPSGVHSWEY WQFEMTQAFP HIANALGMST EDRGVECAPV GAIADAVADG AMGTCLTNEY
     DVTGGKAQDF ANGRAYWSAN TGAFGLVGRI NARYSELGGP ASWLGYPTSS ELKTPDGRGR
     FVTFEHGSIY WTATTGPWEI PGDMLAAWGT QDYEKGSLGY PTGAAVEYNG GLRQQFEGGY
     VFRTSNNQSY WVRGEISKKY AEDGIFAQLG FPTGNEKLIN GGAFQEFEKG NIYWSASTGA
     HVILHGDIFD AWGAKGWEQG EYGFPTSDQT AITAGGQTID FQNGTIRQVN GRIEESR