ID F4Y392_9CYAN Unreviewed; 446 AA.
AC F4Y392;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=LYNGBM3L_71890 {ECO:0000313|EMBL:EGJ28568.1};
OS Moorena producens 3L.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Moorena.
OX NCBI_TaxID=489825 {ECO:0000313|EMBL:EGJ28568.1, ECO:0000313|Proteomes:UP000003959};
RN [1] {ECO:0000313|Proteomes:UP000003959}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3L {ECO:0000313|Proteomes:UP000003959};
RX PubMed=21555588; DOI=10.1073/pnas.1101137108;
RA Jones A.C., Monroe E.A., Podell S., Hess W.R., Klages S., Esquenazi E.,
RA Niessen S., Hoover H., Rothmann M., Lasken R.S., Yates J.R.III.,
RA Reinhardt R., Kube M., Burkart M.D., Allen E.E., Dorrestein P.C.,
RA Gerwick W.H., Gerwick L.;
RT "Genomic insights into the physiology and ecology of the marine filamentous
RT cyanobacterium Lyngbya majuscula.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:8815-8820(2011).
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}.
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DR EMBL; GL890973; EGJ28568.1; -; Genomic_DNA.
DR RefSeq; WP_008191183.1; NZ_MKZR01000001.1.
DR AlphaFoldDB; F4Y392; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_0_3; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000003959; Unassembled WGS sequence.
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..49
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 180..197
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 217..236
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 268..292
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 324..346
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 382..400
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 406..425
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 446 AA; 48171 MW; C0AE89BB605F3E7E CRC64;
MTVSRDKAPT AQETFMQMAQ AAGLRGRLLV TVGLLILARL GVFLPVPGID RARFSAELQN
SPFVGLLDFF SGGGFSALGI FALGILPYIN ASIILQLLTA AIPALENLQK NEGEAGRRKI
GQITRYVALG WSVIQSIGLS LWAQRFAVEP GAFFVFETVL ALTAGSMFVM WLSELITERG
IGNGASLLIF VNIVAVLPRT LGQTIELAQT GGRETVGKVI VLLLVFLVMI VGIVFVQEGS
RRIPIITARR QVGKRLYRER KNYLPLRLNQ GGVMPIIFAS AVLILPTSLA GITSGDNSNG
LLGSINQVLI QIANYLNPNG QTPWVYVAVY LVLILFFSYF YASLIINPVD MSQNLKKMGA
SIPGIRPGRA TSEYIERVLN RLTLLGAIFL GLVAVVPTAV ESATGVTTFR GLGATSLLIL
VGVAIDTAKQ IQTYVISQRY EGMVKQ
//
