ID G0QB99_NANSJ Unreviewed; 446 AA.
AC G0QB99;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|RuleBase:RU000537};
GN ORFNames=J07AB56_13890 {ECO:0000313|EMBL:EGQ40659.1};
OS Nanosalinarum sp. (strain J07AB56).
OC Archaea; Euryarchaeota; Stenosarchaea group; Candidatus Nanohaloarchaea;
OC Nanosalinarum.
OX NCBI_TaxID=889962 {ECO:0000313|EMBL:EGQ40659.1, ECO:0000313|Proteomes:UP000009382};
RN [1] {ECO:0000313|EMBL:EGQ40659.1, ECO:0000313|Proteomes:UP000009382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Narasingarao P., Podell S., Ugalde J.A., Brochier-Armanet C., Emerson J.B.,
RA Brocks J.J., Heidelberg K.B., Banfield J.F., Allen E.E.;
RT "De novo metagenomic assembly reveals abundant novel major lineage of
RT Archaea in hypersaline microbial communities.";
RL ISME J. 0:0-0(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|RuleBase:RU000537}.
CC -!- SUBCELLULAR LOCATION: 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|RuleBase:RU004349}.
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DR EMBL; GL982569; EGQ40659.1; -; Genomic_DNA.
DR AlphaFoldDB; G0QB99; -.
DR HOGENOM; CLU_031763_3_0_2; -.
DR Proteomes; UP000009382; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3370.10; SecY subunit domain; 1.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR030659; SecY_CS.
DR InterPro; IPR023201; SecY_dom_sf.
DR PANTHER; PTHR10906:SF1; DSEC61ALPHA; 1.
DR PANTHER; PTHR10906; SECY/SEC61-ALPHA FAMILY MEMBER; 1.
DR Pfam; PF00344; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU003484};
KW Reference proteome {ECO:0000313|Proteomes:UP000009382};
KW Translocation {ECO:0000256|ARBA:ARBA00023010,
KW ECO:0000256|RuleBase:RU003484};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003484};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003484}.
FT TRANSMEM 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 446 AA; 47652 MW; 7B8800225976DB4E CRC64;
MADWTARIAG YLPSVAEPER EQSLKEMLTW TGVILVLYFT LSSINITPAP FGSGQVSVVN
QALQQLETFQ TLLGASIGSI ITLGIGPIVT ASIVLQMMVG SDLLDWDTNT QSGKQKFQNS
KKILAYAISI VQALGYVLSG TFGSITDPVL IFWVTAQIAL GGVIIILMDE VVQKWGFGSG
VGLFIAAGVS QAIYIRSASF LNGAGEFVGV SSDAVGALPS FAATLDLTAL IPVFSTIAVF
AAVVYMQSMR VEIPLTFGNV RGFGQKWPLK FLYTSNMPVI LIAALVSNVQ IVGSTLSGAN
GSSILGTFSG GQAQSGLVYS APSSQPGLHF FPSIGHLGRQ SVRHLPRTVL HLGLRVRFCS
VFSVLGSDLG AGFEVCRGAD QTDGNEGSRF PEGHARYPEG SRPLHTWFDG SLRFLGRSAG
GARQHHERGW WWNRHLAYCD DSVPSV
//
