ID C4XFZ5_MYCFP Unreviewed; 527 AA.
AC C4XFZ5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465};
GN OrderedLocusNames=MBIO_0802 {ECO:0000313|EMBL:BAH70067.1};
OS Mycoplasmopsis fermentans (strain ATCC 19989 / NBRC 14854 / NCTC 10117 /
OS PG18) (Mycoplasma fermentans).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC Mycoplasmopsis.
OX NCBI_TaxID=496833 {ECO:0000313|EMBL:BAH70067.1, ECO:0000313|Proteomes:UP000006810};
RN [1] {ECO:0000313|EMBL:BAH70067.1, ECO:0000313|Proteomes:UP000006810}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18
RC {ECO:0000313|Proteomes:UP000006810};
RX PubMed=19219498; DOI=10.1007/s00284-009-9362-6;
RA Ishida N., Irikura D., Matsuda K., Sato S., Asano K.;
RT "Molecular cloning and expression of a novel cholinephosphotransferase
RT involved in glycoglycerophospholipid biosynthesis of Mycoplasma
RT fermentans.";
RL Curr. Microbiol. 58:535-540(2009).
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}.
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}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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; AP009608; BAH70067.1; -; Genomic_DNA.
DR AlphaFoldDB; C4XFZ5; -.
DR KEGG; mfp:MBIO_0802; -.
DR PATRIC; fig|496833.3.peg.397; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_1_14; -.
DR Proteomes; UP000006810; 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 PRINTS; PR00303; SECYTRNLCASE.
DR SUPFAM; SSF103491; Preprotein translocase SecY subunit; 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:UP000006810};
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 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 112..133
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 154..177
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 197..218
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 225..242
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 262..287
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 361..379
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 410..432
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 438..461
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 527 AA; 59480 MW; 9A0428F5DF0DF1E4 CRC64;
MVVYYIIIKY FIRDKVELVF AMKVRVEYMK KFFSNVGFKI SKFFYNFKNK WIVFWSTKEI
TKKLLYTLLL LSIYILMTTI KAPFVKLSDV NINDDPFLNT LNLVGGGGLK NFSLAALGIS
PFINASLIMS LLQTKLFPPI QKLSQSGPQG RRKLNIITRI LTLFIAFPQA ILLTKSLSLG
DNPFIGFTPI QKLPREVTIY LILPLILIGG SLFSLFIAEQ ITDKGLGNGT SLIIFVGIAF
QLQSQFKGAF SLFVGSESTA AIFVGALKFL TYLFVYFALL FIIALVYNAE RHVPIQQIGA
GRSRNINEMG KLPIKLNPGG IMPIIFASML VSFPIMISRI LPKGNSGKLW IEANMQFTQP
LGLSLLILIT FFFSYIIGLQ QSRIDKISED FAKNSTFIPG IRPGEETEDY LIGVVLRLCT
FSGFYLVFLA SFQYIMILWL QIPAIVSFGG TGMMILVSVA LETIQQFMAR RKSQHLAKQK
RLSKEAADVL NFQNKYQEND PFATNDQKSE DVSKEYDKYK NGDGLLW
//
