ID A0A367B8H9_9ACTN Unreviewed; 436 AA.
AC A0A367B8H9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=DQ237_06920 {ECO:0000313|EMBL:RBY97285.1};
OS Blastococcus sp. TF02-8.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=2250574 {ECO:0000313|EMBL:RBY97285.1, ECO:0000313|Proteomes:UP000252403};
RN [1] {ECO:0000313|EMBL:RBY97285.1, ECO:0000313|Proteomes:UP000252403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02-8 {ECO:0000313|EMBL:RBY97285.1,
RC ECO:0000313|Proteomes:UP000252403};
RA Ennis N., Dharumadurai D., Sevigny J., Hall J., Morris K., Simpson S.,
RA Thomas W.K., Tisa L.S.;
RT "Genome Sequence of Blastococcus sp. TF02-8.";
RL Submitted (JUL-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBY97285.1}.
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DR EMBL; QOHK01000002; RBY97285.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367B8H9; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000252403; Unassembled WGS sequence.
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:UP000252403};
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 74..98
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 118..137
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 185..204
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 216..235
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 263..284
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 316..336
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 401..419
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 436 AA; 47540 MW; 3500D64C7602C080 CRC64;
MLQAFAAAFR TPDLRRKLLF SLAIIAVYRL GAQVPGPGVS VKAINSCLEQ AQNSDQRDIY
SLVNLFSGGA LLKLSIFALG IMPYITASII VQLLVVVIPR FEMLKKEGQS GQAKLTQYTR
YLTIALAILQ STGIIALARS GQLFPNCSEP IIPSDSVWTT VILVVALTAG TALIMWLGEL
LTDKGIGNGM SVLIFTSIAA RIPAEGGAIL QARGGVVFAV VCVIAVLIIG TVVYVEQAQR
RIPVQYAKRM VGRRMYGGTS TYLPLKVNQA GVIPVIFASS LLYLPQLITQ LQGNETGTVR
RFVENYIISQ SSPVHVALYF GLIVFFTYFY VSITFNPEER ADDMKRYGGF IPGIRPGRPT
AEYLQYVLSR ITLPGSIYLG LVAVLPNLFL SLTQPGQNQN FPFGGTAVLI MVGVGLETVK
QIETQLNQRN YEGFLK
//