SECY_MYCGA
ID SECY_MYCGA Reviewed; 498 AA.
AC O52351;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465};
GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; Synonyms=recY;
GN OrderedLocusNames=MYCGA0700; ORFNames=MGA_0740;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RX PubMed=10867916;
RA Skamrov A.V., Gol'dman M.A., Feoktistova E.S., Bibilashvili R.S.;
RT "Determination and analysis of the nucleotide sequence of a segment of a
RT Mycoplasma gallisepticum strain A5969 chromosome, containing operons S10
RT and rrn23-5.";
RL Mol. Biol. (Mosk.) 34:390-396(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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:0000255|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:0000255|HAMAP-
CC Rule:MF_01465}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01465};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01465}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000255|HAMAP-
CC Rule:MF_01465}.
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DR EMBL; AF036708; AAB95406.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56420.1; -; Genomic_DNA.
DR RefSeq; WP_011113299.1; NC_004829.2.
DR AlphaFoldDB; O52351; -.
DR SMR; O52351; -.
DR GeneID; 57203346; -.
DR KEGG; mga:MGA_0740; -.
DR HOGENOM; CLU_030313_0_1_14; -.
DR OMA; FAMWLGE; -.
DR OrthoDB; 1567535at2; -.
DR Proteomes; UP000001418; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; -; 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 PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SSF103491; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..498
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131734"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465"
FT REGION 478..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 13
FT /note="K -> R (in Ref. 1; AAB95406)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="S -> T (in Ref. 1; AAB95406)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="I -> V (in Ref. 1; AAB95406)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="A -> V (in Ref. 1; AAB95406)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="Q -> K (in Ref. 1; AAB95406)"
FT /evidence="ECO:0000305"
FT CONFLICT 490
FT /note="D -> N (in Ref. 1; AAB95406)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 498 AA; 55045 MW; 2EB3ED5FD63CE1F2 CRC64;
MAKTNSKNLL GQKIIKLLRN RDFVISVFVT LFLILLFRVI SVIPLPGITI SQNKNNLNNG
VSDFFDLFNL LGGGGLSQLS LFAVGISPYI SAQIIMQLLS TDLIPPLSKL AKSGELGRRR
IELITRFVTL PFAVVQAFAI IALINNQRNG AIRFENGGIL HQAFYIVTMT AGTYIGIFIG
DIISKKGVGN GITLLILSGI LARLPDGFIV MYRVLGGVII STNPILTSAI NFSLYFLAFL
VLLLAISFVN SSTRRIPIQQ TGEGMVLGNE KLPYLPIKLN AAGVIPVIFA SSIMSIPITI
AEFQPQSEAR WFVEDYLSLR TPVGISLYVI LIIIFTFFYS YIQINPEQLA ENFNKSHKFI
PGVRPGLDTE KHITKVLMRI NFIGAPFLAI VAVIPYIISL VLNVPTTLSL GGTGIIIMVS
ASMELYRSLR SAATTTSYQR LRKDIANRIE AELSLNDYMN KPNLEHDQYG LLGQHKKVEP
TQDKKKNPSD PLEVSQLW
