ID B1VEX5_CORU7 Unreviewed; 471 AA.
AC B1VEX5;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=cu0354 {ECO:0000313|EMBL:CAQ04314.1};
OS Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ04314.1, ECO:0000313|Proteomes:UP000001727};
RN [1] {ECO:0000313|EMBL:CAQ04314.1, ECO:0000313|Proteomes:UP000001727}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727};
RX PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J.,
RA Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M.,
RA Puehler A.;
RT "The lifestyle of Corynebacterium urealyticum derived from its complete
RT genome sequence established by pyrosequencing.";
RL J. Biotechnol. 136:11-21(2008).
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}.
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DR EMBL; AM942444; CAQ04314.1; -; Genomic_DNA.
DR AlphaFoldDB; B1VEX5; -.
DR STRING; 504474.cu0354; -.
DR KEGG; cur:cu0354; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_0_11; -.
DR Proteomes; UP000001727; Chromosome.
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: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 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:UP000001727};
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 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 94..121
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 142..161
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 181..202
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 214..234
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 240..259
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 344..363
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 403..422
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 434..454
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 471 AA; 50888 MW; ACEE3699DAD6330A CRC64;
MAHALRHRPC DNSRGHHSAG PPTQEASLSA ITGAFKNVDL RKKILFTLAM IILYRIGSQI
PTPGVDYANI TKQISELTES SAVYSLINLF SGGALLQLSI FAIGIMPYIT ASIIVQLLTV
VIPKFEQLKK EGQTGQAKMT EYTRYLTVAL ALLQSAGIVA LADREQLLGQ GIPVLKDEVG
IFGLIVMVLI MTSGAVLVMW LGELITDRGV GNGMSLLIMA GIATTLPGEG VSILSNSGGF
IFGAVVFGML LLIVGVVFVE QGQRRIPVQY AKRMIGRRQY GETSTYLPLK VNQAGVIPVI
FASSLLTVPI LITQIIQSGA AAGEDVANNW WNRNVMTVLQ NPAAWQYILV YLALIIFFSF
FYVSVQYDPY DQADNMKKYG GFIPGIRPGR PTAEYLGYVM NRLLVVGSLY LGIIAVLPNI
LINLGVDTSQ ASGGGMPFGG TAVLILVSVA LTTVKQIESQ MMQANYEGFL K
//
