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Database: UniProt
Entry: R6I4H5_9FIRM
LinkDB: R6I4H5_9FIRM
Original site: R6I4H5_9FIRM 
ID   R6I4H5_9FIRM            Unreviewed;       424 AA.
AC   R6I4H5;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=BN556_01644 {ECO:0000313|EMBL:CDB44200.1};
OS   Firmicutes bacterium CAG:240.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263013 {ECO:0000313|EMBL:CDB44200.1, ECO:0000313|Proteomes:UP000018051};
RN   [1] {ECO:0000313|EMBL:CDB44200.1, ECO:0000313|Proteomes:UP000018051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:240 {ECO:0000313|Proteomes:UP000018051};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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:CDB44200.1}.
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DR   EMBL; CBDR010000195; CDB44200.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6I4H5; -.
DR   Proteomes; UP000018051; 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:UP000018051};
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        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        118..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        147..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        175..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        209..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        300..318
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        359..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        389..410
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ   SEQUENCE   424 AA;  46339 MW;  1B1BD39FA621C9A0 CRC64;
     MLQTMRNAWK IDDLRHKILF TLVIILLYRL GNAVPVPYVN IDALNGYFAQ MQNTVLGLLN
     VMSGGAFSNA TIFALSIQPY INASIIIQLL CIAIPALERM SKEEGEEGKK KIASITRYTT
     VAIGLIQGFA YYYMIMKSGF LTADGQGVWA AIVIILTFTS GSALIMWLGE QITEFGIGNG
     ISIILFASIV SRFPPSLYQM ITNTVNGTVA WWVNVLLLLG ALAMIVLIVL INDSERRIPV
     QYAKRVVGRK MYGGQSTHLP MKVNMSGVLP IIFAQSIATL PATIAAFTGH SDSAWASTTS
     IPYAIIYFLL IIFFAYFYST IQFNPVEVAN NLKKNGGYIP GFRPGKPTSE FIKKVLNKIT
     LFGAIYLGII AIVPILISHF STSASLSGIS LGGTSIIIVV GVALETVRAL EAQMLMRNYK
     GFLS
//
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