ID B8HMS2_CYAP4 Unreviewed; 436 AA.
AC B8HMS2;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
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 OrderedLocusNames=Cyan7425_1310 {ECO:0000313|EMBL:ACL43687.1};
OS Cyanothece sp. (strain PCC 7425 / ATCC 29141).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Cyanothecaceae;
OC Cyanothece.
OX NCBI_TaxID=395961 {ECO:0000313|EMBL:ACL43687.1};
RN [1] {ECO:0000313|EMBL:ACL43687.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PCC 7425 {ECO:0000313|EMBL:ACL43687.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Meineke L., Brettin T.,
RA Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Ovchinnikova G., Liberton M., Stoeckel J., Banerjee A., Singh A., Page L.,
RA Sato H., Zhao L., Sherman L., Pakrasi H., Richardson P.;
RT "Complete sequence of chromosome Cyanothece sp. PCC 7425.";
RL Submitted (JAN-2009) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01465}. Cellular thylakoid membrane {ECO:0000256|HAMAP-
CC Rule:MF_01465}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01465}. Membrane {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU003484}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141, 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; CP001344; ACL43687.1; -; Genomic_DNA.
DR AlphaFoldDB; B8HMS2; -.
DR STRING; 395961.Cyan7425_1310; -.
DR KEGG; cyn:Cyan7425_1310; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_0_3; -.
DR OrthoDB; 9809248at2; -.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01465};
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}; Thylakoid {ECO:0000256|HAMAP-Rule:MF_01465};
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 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 187..204
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 273..294
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 314..336
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 372..390
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 396..415
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 436 AA; 46900 MW; 36684B2F7C2D52AF CRC64;
MVVSRGKAPT AQETFAQMAQ AAGLRGRLLV TIGLLILVRL GIYLPVPGID RQVFAQTIQN
NPVIGFLDIF SGGGLSALGI FALGILPYIN ASIILQLLTA ALPSLERLQK DEGEAGRRKI
SQITRYVALV WAIIQSTGIA IWVSSTPGAV FNPGPIFIGE MVLALTAGSM FVMWVSELIT
ERGVGNGASL LIFLSIVAYL PTSINQTIEL AQSGGSVGGV VILALVFLAM IVGIVFVQEG
TRRIPIISAR RQVGRRLYRE QTSYLPLRLN QGGVMPIIFA SAVLVLPSYL AGFTKNETVA
QIANYITPNG PTPWLYVLFY LVLILFFSYF YASLVVNPVD MAQNLKKMGA SIPGIRPGRA
TSEYVEGVLN RLTFLGAIFL GAVAIIPTAV ESATRVTTFR GFGATSLLIL VGVAIDTAKQ
IQTYVISQRY EGMVKQ
//
