ID A0A1U7IMI3_9CYAN Unreviewed; 434 AA.
AC A0A1U7IMI3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=NIES2119_10195 {ECO:0000313|EMBL:OKH38394.1};
OS Phormidium ambiguum IAM M-71.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Oscillatoriaceae; Phormidium.
OX NCBI_TaxID=454136 {ECO:0000313|EMBL:OKH38394.1, ECO:0000313|Proteomes:UP000185860};
RN [1] {ECO:0000313|EMBL:OKH38394.1, ECO:0000313|Proteomes:UP000185860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAM M-71 {ECO:0000313|EMBL:OKH38394.1,
RC ECO:0000313|Proteomes:UP000185860};
RA Zhu T., Hou S., Lu X., Hess W.R.;
RT "Draft Genome Sequences of Nine Cyanobacterial Strains from Diverse
RT Habitats.";
RL Submitted (NOV-2016) 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: 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:OKH38394.1}.
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DR EMBL; MRCE01000008; OKH38394.1; -; Genomic_DNA.
DR RefSeq; WP_073593358.1; NZ_MRCE01000008.1.
DR AlphaFoldDB; A0A1U7IMI3; -.
DR STRING; 454136.NIES2119_10195; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000185860; 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}; Reference proteome {ECO:0000313|Proteomes:UP000185860};
KW 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..102
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 123..142
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 186..205
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 274..295
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 315..338
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 371..389
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 395..413
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 434 AA; 46889 MW; 7AA34317937543EA CRC64;
MMISREKAPT AQETFAQMAQ AAGLRGRLLV TLGLLILVRL GVFLPVPGIN REAFRAQVQN
SPLVGLLDLF SGGGIVALGI FALGILPFIN ASIIMQLLTA ALPSLENLQK NEGEAGRRKI
SQWTRYVAVV WAVIQSIGIS IWVSPFAEAP NPGFWFFAKT VIALTAGSMF VMWVSELITE
RGLGNGASLL IFLNIVAVVP KSFAATIDLA QTGGREIVGK VIILLVVFLV MIVGIVFVQE
GSRRIPIISA RRQVGRKLYL EKSSYLPLRL NQGGVMPIIF ASAVLFLPAS LANFVQNETL
NKIAATYLNP GSPVYVITYL VLILFFSYFY ASLIVNPVDL AQNLKKMGSS IPGIRPGKAT
SEYVERVLNR LTFLGAVFLG VVAIVPTAVE SATVGTFRGL GATSLLILVG VAIDTSKQIQ
TYVISQRYEG MVKE
//
