SECY_CORGL
ID SECY_CORGL Reviewed; 440 AA.
AC P38376;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465};
GN OrderedLocusNames=Cgl0555, cg0647;
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 [GENOMIC DNA].
RC STRAIN=MJ233;
RX PubMed=8112597; DOI=10.1016/0378-1119(94)90530-4;
RA Kobayashi M., Fugono N., Asai Y., Inui M., Vertes A.A., Kurusu Y.,
RA Yukawa H.;
RT "Cloning and sequencing of the secY homolog from Coryneform bacteria.";
RL Gene 139:99-103(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Berens S., Kalinowski J., Puhler A.;
RT "The role of Corynebacterium glutamicum secretion genes secD, secF and secG
RT in transporting the Streptomyces griseus alpha-amylase.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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: The central subunit of the protein translocation channel
CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two
CC domains form a lateral gate at the front which open onto the bilayer
CC between TMs 2 and 7, and are clamped together by SecE at the back. The
CC channel is closed by both a pore ring composed of hydrophobic SecY
CC resides and a short helix (helix 2A) on the extracellular side of the
CC membrane which forms a plug. The plug probably moves laterally to allow
CC the channel to open. The ring and the pore may move independently.
CC {ECO:0000255|HAMAP-Rule:MF_01465}.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of SecY, SecE and SecG subunits. The heterotrimers can form
CC oligomers, although 1 heterotrimer is thought to be able to translocate
CC proteins. Interacts with the ribosome. Interacts with SecDF, and other
CC proteins may be involved. Interacts with SecA. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01465};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01465}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
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DR EMBL; D14162; BAA03207.1; -; Genomic_DNA.
DR EMBL; AF331925; AAK18191.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB97948.1; -; Genomic_DNA.
DR EMBL; BX927149; CAF19262.1; -; Genomic_DNA.
DR PIR; I40340; I40340.
DR RefSeq; NP_599793.1; NC_003450.3.
DR RefSeq; WP_003854402.1; NC_006958.1.
DR AlphaFoldDB; P38376; -.
DR SMR; P38376; -.
DR STRING; 196627.cg0647; -.
DR GeneID; 58309525; -.
DR KEGG; cgb:cg0647; -.
DR KEGG; cgl:Cgl0555; -.
DR PATRIC; fig|196627.13.peg.548; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_0_11; -.
DR OMA; FAMWLGE; -.
DR Proteomes; UP000000582; Chromosome.
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:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.3370.10; -; 1.
DR HAMAP; MF_01465; SecY; 1.
DR InterPro; IPR026593; SecY.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..440
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131720"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 116..135
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 213..233
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ SEQUENCE 440 AA; 47903 MW; 3C8871F57A6825E2 CRC64;
MSAIIQAFKD ADLRKKIFFT IAMIVLYRIG AQIPSPGVDY ATISGRLRDL TQDQSSVYSL
INLFSGGALL QLSIFAIGIM PYITASIIVQ LLTVVIPHFE ELKKEGQSGQ AKMMQYTRYL
TVALALLQSS GIVALADREQ LLGAGIRVLS ADRNFFDLIV LVITMTAGAV LVMWMGELIT
EKGVGNGMSL LIFAGIATRL PTDGMNILGN SGGVVFAVVL ASVLILVIGV VFVEQGQRRI
PVQYAKRMVG RRQYGGSSTY LPLKVNQAGV IPVIFASSLI YMPVLITQIV NSGSLEVSDN
WWQRNIIAHL QTPSSWQYIV LYFALTIFFS YFYVSVQYDP AEQAENMKKY GGFIPGIRPG
RPTAEYLGFV MNRLLFVGSL YLAVIAVLPN IMLDLGVDAG SAGATPFGGT AILILVSVAL
TTVKQIESQL LQSNYEGLLK
