ID D5E4X7_MYCCM Unreviewed; 475 AA.
AC D5E4X7;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000256|HAMAP-Rule:MF_01465,
GN ECO:0000313|EMBL:ADE19924.1};
GN OrderedLocusNames=MCRO_0149 {ECO:0000313|EMBL:ADE19924.1};
OS Mycoplasma crocodyli (strain ATCC 51981 / MP145).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=512564 {ECO:0000313|EMBL:ADE19924.1, ECO:0000313|Proteomes:UP000001845};
RN [1] {ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RA Glass J.I., Durkin A.S., Hostetler J., Jackson J., Johnson J., May M.A.,
RA Paralanov V., Radune D., Szczypinski B., Brown D.R.;
RT "The complete genome of Mycoplasma crocodyli MP145.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MP145;
RA Ma Z., Wang X., Liu H.;
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ADE19924.1, ECO:0000313|Proteomes:UP000001845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51981 / MP145 {ECO:0000313|Proteomes:UP000001845};
RX PubMed=21460083; DOI=10.1128/JB.00309-11;
RA Brown D.R., Farmerie W.G., May M., Benders G.A., Durkin A.S., Hlavinka K.,
RA Hostetler J., Jackson J., Johnson J., Miller R.H., Paralanov V., Radune D.,
RA Szczypinski B., Glass J.I.;
RT "Genome sequences of Mycoplasma alligatoris A21JP2T and Mycoplasma
RT crocodyli MP145T.";
RL J. Bacteriol. 193:2892-2893(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|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; CP001991; ADE19924.1; -; Genomic_DNA.
DR AlphaFoldDB; D5E4X7; -.
DR STRING; 512564.MCRO_0149; -.
DR KEGG; mcd:MCRO_0149; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_1_14; -.
DR Proteomes; UP000001845; 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; 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:UP000001845};
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 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 84..105
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 126..145
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 171..192
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 199..217
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 237..261
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 335..353
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 384..409
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 475 AA; 52317 MW; 169BE8498D466236 CRC64;
MFFRRIKKLG ITKLFYKLRA AWVNFWSTKD VTKKIMYTLL LISIYVIGTT ITSPFVKINA
GRSINDDSFL NTLNLVGGGG LNQFSIFALG ISPFINASLV MMILQSKLFP PVYKLSQSGP
QGRRKINVIT RVITLVISYP QALFLTKSLS AGGARSAFIS IVPAFGMSQD LISYFILPLI
LVAASLFVLF ISEQVTNKGI GNGTSLIIFC GIAMRLPSQF SSAYKILVGD LKSEGTFVGI
INFSTYILIY LVVLMIITIV YNAERHIPIQ QTGAGRSRNI KEMGKLPIKL NPGGIMPIIF
AMMVLSFPTM IANVFPGNSP AKFWINHNLQ FTQPLGLSLL ILITFVFSLL MGLQQSRVDK
IAEDFAKSST FVPGLRPGEE TQDYLIGVVF RLSLFSGFYL VILVSMQFIQ IITGILAPQI
AFGGTGMVIL VSVALETFSQ VSARRKSTKL AKAKRVTKKS FESNSSNKKG DGLLW
//
