SECE_STRVG
ID SECE_STRVG Reviewed; 93 AA.
AC P36691;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
GN Name=secE {ECO:0000255|HAMAP-Rule:MF_00422};
OS Streptomyces virginiae.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces virginiae group.
OX NCBI_TaxID=1961;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8675024; DOI=10.1016/0378-1119(96)00067-4;
RA Katayama M., Sakai Y., Okamoto S., Ihara F., Nihira T., Yamada Y.;
RT "Gene organization in the ada-rplL region of Streptomyces virginiae.";
RL Gene 171:135-136(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MAFF10-06014;
RX PubMed=1309760; DOI=10.1016/s0021-9258(18)48400-1;
RA Okamoto S., Nihirra T., Kataoka H., Suzuki A., Yamada Y.;
RT "Purification and molecular cloning of a butyrolactone autoregulator
RT receptor from Streptomyces virginiae.";
RL J. Biol. Chem. 267:1093-1098(1992).
CC -!- FUNCTION: Essential subunit of the Sec protein translocation channel
CC SecYEG. Clamps together the 2 halves of SecY. May contact the channel
CC plug during translocation. {ECO:0000255|HAMAP-Rule:MF_00422}.
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_00422}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00422};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00422}.
CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000255|HAMAP-
CC Rule:MF_00422}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09300.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D50624; BAA09300.1; ALT_INIT; Genomic_DNA.
DR EMBL; D10468; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_030388883.1; NZ_LGUV01000155.1.
DR AlphaFoldDB; P36691; -.
DR SMR; P36691; -.
DR STRING; 1961.JOAK01000021_gene7140; -.
DR eggNOG; COG0690; Bacteria.
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:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0009306; P:protein secretion; 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; 1.20.5.1030; -; 1.
DR HAMAP; MF_00422; SecE; 1.
DR InterPro; IPR005807; SecE_bac.
DR InterPro; IPR038379; SecE_sf.
DR InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR PANTHER; PTHR33910; PTHR33910; 1.
DR Pfam; PF00584; SecE; 1.
DR TIGRFAMs; TIGR00964; secE_bact; 1.
DR PROSITE; PS01067; SECE_SEC61G; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..93
FT /note="Protein translocase subunit SecE"
FT /id="PRO_0000104187"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 49
FT /note="R -> P (in Ref. 2; D10468)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="V -> L (in Ref. 2; D10468)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="G -> R (in Ref. 2; D10468)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 93 AA; 10447 MW; 63000CD09CE67B83 CRC64;
MTDALGSIDM PDAEDETREK KARKGGKRGK KGPLGRLALF YRQIVAELRK VVWPTRNQLT
TYTTVVIVFV VIMIGLVTVI DFGFEKAIKF VFG