ID E6X2K8_NITSE Unreviewed; 59 AA.
AC E6X2K8;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Protein translocase subunit SecE {ECO:0000256|HAMAP-Rule:MF_00422};
GN Name=secE {ECO:0000256|HAMAP-Rule:MF_00422};
GN OrderedLocusNames=Nitsa_1970 {ECO:0000313|EMBL:ADV47213.1};
OS Nitratifractor salsuginis (strain DSM 16511 / JCM 12458 / E9I37-1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurovaceae; Nitratifractor.
OX NCBI_TaxID=749222 {ECO:0000313|EMBL:ADV47213.1, ECO:0000313|Proteomes:UP000008633};
RN [1] {ECO:0000313|EMBL:ADV47213.1, ECO:0000313|Proteomes:UP000008633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1
RC {ECO:0000313|Proteomes:UP000008633};
RX PubMed=21886859;
RA Anderson I., Sikorski J., Zeytun A., Nolan M., Lapidus A., Lucas S.,
RA Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Ngatchou-Djao O.D., Rohde M., Tindall B.J., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Nitratifractor salsuginis type strain (E9I37-
RT 1).";
RL Stand. Genomic Sci. 4:322-330(2011).
RN [2] {ECO:0000313|Proteomes:UP000008633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16511 / JCM 12458 / E9I37-1
RC {ECO:0000313|Proteomes:UP000008633};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Zeytun A.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Schuetze A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Nitratifractor salsuginis DSM 16511.";
RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00422}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00422}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00422}.
CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000256|HAMAP-
CC Rule:MF_00422}.
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DR EMBL; CP002452; ADV47213.1; -; Genomic_DNA.
DR RefSeq; WP_013554898.1; NC_014935.1.
DR AlphaFoldDB; E6X2K8; -.
DR STRING; 749222.Nitsa_1970; -.
DR KEGG; nsa:Nitsa_1970; -.
DR eggNOG; COG0690; Bacteria.
DR HOGENOM; CLU_113663_7_2_7; -.
DR OMA; DWILFHS; -.
DR Proteomes; UP000008633; Chromosome.
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; Preprotein translocase secy subunit; 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 NCBIfam; TIGR00964; secE_bact; 1.
DR PANTHER; PTHR33910; PROTEIN TRANSLOCASE SUBUNIT SECE; 1.
DR PANTHER; PTHR33910:SF1; PROTEIN TRANSLOCASE SUBUNIT SECE; 1.
DR Pfam; PF00584; SecE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00422};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00422};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00422};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_00422}; Reference proteome {ECO:0000313|Proteomes:UP000008633};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_00422};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00422};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00422};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00422}.
FT TRANSMEM 29..55
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00422"
SQ SEQUENCE 59 AA; 6535 MW; C25913E7B671E743 CRC64;
MNKLIKFIKD AKVELDKVIF PTKVQVRQAF VAVVLVVTVI SIFLALVDML MSAIVSSTL
//