ID F2I7T6_AERUA Unreviewed; 432 AA.
AC F2I7T6; A0A9Q4D944;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465,
GN ECO:0000313|EMBL:AEA01285.1};
GN OrderedLocusNames=HMPREF9243_0528 {ECO:0000313|EMBL:AEA01285.1};
OS Aerococcus urinae (strain CCUG 59500 / ACS-120-V-Col10a).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Aerococcus;
OC Aerococcus incertae sedis.
OX NCBI_TaxID=2976812 {ECO:0000313|EMBL:AEA01285.1, ECO:0000313|Proteomes:UP000008129};
RN [1] {ECO:0000313|Proteomes:UP000008129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-120-V-Col10a {ECO:0000313|Proteomes:UP000008129};
RA Durkin A.S., Madupu R., Radune D., Hostetler J., Torralba M., Gillis M.,
RA Methe B., Sutton G., Nelson K.E.;
RT "Complete genome sequence of Aerococcus urinae strain ACS-120-V-Col10a.";
RL Submitted (FEB-2011) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01465}.
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DR EMBL; CP002512; AEA01285.1; -; Genomic_DNA.
DR RefSeq; WP_013669519.1; NZ_JAOTMI010000009.1.
DR AlphaFoldDB; F2I7T6; -.
DR STRING; 866775.HMPREF9243_0528; -.
DR KEGG; aur:HMPREF9243_0528; -.
DR PATRIC; fig|866775.3.peg.499; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_1_9; -.
DR Proteomes; UP000008129; Chromosome.
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: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 {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:UP000008129};
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 20..44
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 148..167
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 179..204
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 259..280
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 311..330
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 368..390
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 396..414
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 432 AA; 47701 MW; 0EDF559D2EE21999 CRC64;
MFSTLKQAFK DKNIRGRIFF TLWMLIVFRI GSHITVPFVN AGAVSTLANS GLFGLLNTFG
GGALASYSIF SLGVSPYITA SIVIQLLQME IVPSFTEWSK QGEVGRRKLN KWTRYFAVAI
AFFQSLALSL GFNSLAQFGL IQNPSTTTYL FIALIMTAGS MFVTWIGEQI TQYGVGNGTS
LIIFAGIVSR VPTEIVAFVS SKLLKAEGNA LVQNGLLALA FILIMILIIT FVVFINQAER
RIPVRYSKRA NSANQRAHLP LKINSAGVIP VIFASSLIMV PQTILNFFRA SHGEAEWFKL
VSRIFSLQDP LGITLYAVTI ILFTFFYAHI QINPERVAEN FQKSGAYIPS VRPGLATEQF
ISTVLNRLSF FGALFLMAIA TAPLVISYVL DMSQRVALSG TSLLIVVGVA LDTYKQIEGR
LIKHRYIGFI RE
//
