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Database: UniProt
Entry: A0A239TV68_9FIRM
LinkDB: A0A239TV68_9FIRM
Original site: A0A239TV68_9FIRM 
ID   A0A239TV68_9FIRM        Unreviewed;       418 AA.
AC   A0A239TV68;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000256|ARBA:ARBA00039733, ECO:0000256|HAMAP-Rule:MF_01465};
GN   Name=secY {ECO:0000256|HAMAP-Rule:MF_01465,
GN   ECO:0000313|EMBL:SNV01690.1};
GN   ORFNames=SAMEA4364220_01476 {ECO:0000313|EMBL:SNV01690.1};
OS   Megamonas hypermegale.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC   Megamonas.
OX   NCBI_TaxID=158847 {ECO:0000313|EMBL:SNV01690.1, ECO:0000313|Proteomes:UP000215383};
RN   [1] {ECO:0000313|EMBL:SNV01690.1, ECO:0000313|Proteomes:UP000215383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10570 {ECO:0000313|EMBL:SNV01690.1,
RC   ECO:0000313|Proteomes:UP000215383};
RG   Pathogen Informatics;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537}.
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_01465}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01465}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003484}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU003484}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family.
CC       {ECO:0000256|ARBA:ARBA00005751, ECO:0000256|HAMAP-Rule:MF_01465,
CC       ECO:0000256|RuleBase:RU004349}.
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DR   EMBL; LT906446; SNV01690.1; -; Genomic_DNA.
DR   RefSeq; WP_027889369.1; NZ_NFIW01000005.1.
DR   AlphaFoldDB; A0A239TV68; -.
DR   GeneID; 78507474; -.
DR   eggNOG; COG0201; Bacteria.
DR   OrthoDB; 9809248at2; -.
DR   Proteomes; UP000215383; Chromosome 1.
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; 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:SF2; PREPROTEIN TRANSLOCASE SUBUNIT SCY2, 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 {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01465};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01465}; Reference proteome {ECO:0000313|Proteomes:UP000215383};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW   Rule:MF_01465};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01465};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01465};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01465}.
FT   TRANSMEM        18..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        115..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        143..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        174..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        203..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        301..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        356..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        383..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   418 AA;  45783 MW;  EBD76343A3585D52 CRC64;
     MLSALSNILK ITELRQKIVF TLIMFAIFRL GTHIPVPGVN PAVLEQLFNS GNLFGLLDLF
     SGGALSKFSL FAMSITPYIN ASIIIQLLTV VIPTLEQWSK EGEEGHKKIT KTTRYLTVVL
     AFLQAIGMSI GLKQAIINPS FTSIFIIAIT LTAGTVFLMW IGEQITAHGV GNGISLIIFA
     GIVAALPHNL STIYNYLQAG TISYFNVLFF GIIALAMIVF VIAINEGQRR VPVSYAKRVV
     GRKTYGGHST HIPLKVNQAG VIPIIFASSV LMFPPTIAQF VQNPTIKQIA DYFQWGTPFQ
     SALYALLIIF FTYFYTAVTF KIPDLADNLK KYGGFIPGIR PGQATADYLD RIMTRITLAG
     AFFLAFIAIL PTMIAGATHI EGIHFGGTAL LIVVGVALNT MQQIESMVVM RHYEGFMK
//
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