ID SECY_MYCGE Reviewed; 475 AA.
AC P47416;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; OrderedLocusNames=MG170;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
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; L43967; AAC71388.1; -; Genomic_DNA.
DR PIR; H64218; H64218.
DR RefSeq; WP_009885855.1; NZ_AAGX01000007.1.
DR AlphaFoldDB; P47416; -.
DR SMR; P47416; -.
DR STRING; 243273.MG_170; -.
DR KEGG; mge:MG_170; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_1_14; -.
DR InParanoid; P47416; -.
DR OrthoDB; 9809248at2; -.
DR BioCyc; MGEN243273:G1GJ2-194-MONOMER; -.
DR Proteomes; UP000000807; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR Gene3D; 1.10.3370.10; SecY subunit domain; 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 NCBIfam; TIGR00967; 3a0501s007; 1.
DR PANTHER; PTHR10906:SF9; PREPROTEIN TRANSLOCASE SUBUNIT SCY1, CHLOROPLASTIC; 1.
DR PANTHER; PTHR10906; SECY/SEC61-ALPHA FAMILY MEMBER; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR PRINTS; PR00303; SECYTRNLCASE.
DR SUPFAM; SSF103491; Preprotein translocase SecY subunit; 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..475
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131735"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 385..405
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
SQ SEQUENCE 475 AA; 51845 MW; 073DAE0FC529DFAF CRC64;
MQTVSSPKQK LNFGQRLLTL LQNRDFMVSL VLTVVLLILF RVLAIIPLPG IRINESVLDR
NSNDFFSLFN LLGGGGLNQL SLFAVGISPY ISAQIIMQLL STDLIPPLSK LVNSGEVGRR
KIEMITRIIT LPFALVQAFA VIQIATNAGT GSSPISLANS GSEFIAFYII AMTAGTYMAV
FLGDTISKKG VGNGITLLIL SGILSQLPQG FIAAYNVLSG IVITLTPQLT AAISFFIYFL
AFLVLLFATT FITQATRKIP IQQSGQGLVS EVKTLPYLPI KVNAAGVIPV IFASSIMSIP
VTIAQFQPQT ESRWFVEDYL SLSTPVGIFL YAVLVILFSF FYSYIQINPE RLAKNFEKSG
RFIPGIRPGN DTEKHIARVL IRINFIGAPF LTVIAIIPYI VSYFIRLPNS LSLGGTGIII
IVTAVVEFIS ALRSAATATN YQQLRRNLAI EVQQTAKQDS LEQLQKEAPG IGNLW
//
