ID SECY_MYCPN Reviewed; 477 AA. AC Q59548; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Protein translocase subunit SecY {ECO:0000255|HAMAP-Rule:MF_01465}; GN Name=secY {ECO:0000255|HAMAP-Rule:MF_01465}; GN OrderedLocusNames=MPN_184; ORFNames=MP647; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8604303; DOI=10.1093/nar/24.4.628; RA Hilbert H., Himmelreich R., Plagens H., Herrmann R.; RT "Sequence analysis of 56 kb from the genome of the bacterium Mycoplasma RT pneumoniae comprising the dnaA region, the atp operon and a cluster of RT ribosomal protein genes."; RL Nucleic Acids Res. 24:628-639(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U34795; AAC43697.1; -; Genomic_DNA. DR EMBL; U00089; AAB96295.1; -; Genomic_DNA. DR PIR; S62824; S62824. DR RefSeq; NP_109872.1; NC_000912.1. DR RefSeq; WP_010874541.1; NC_000912.1. DR AlphaFoldDB; Q59548; -. DR SMR; Q59548; -. DR STRING; 272634.MPN_184; -. DR EnsemblBacteria; AAB96295; AAB96295; MPN_184. DR KEGG; mpn:MPN_184; -. DR PATRIC; fig|272634.6.peg.202; -. DR HOGENOM; CLU_030313_0_1_14; -. DR OrthoDB; 9809248at2; -. DR BioCyc; MPNE272634:G1GJ3-297-MONOMER; -. DR Proteomes; UP000000808; 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; Membrane; Protein transport; Reference proteome; KW Translocation; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1..477 FT /note="Protein translocase subunit SecY" FT /id="PRO_0000131736" FT TRANSMEM 28..48 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 67..89 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 130..150 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 196..216 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 234..254 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 286..306 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 329..349 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 387..407 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" FT TRANSMEM 413..433 FT /note="Helical" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01465" SQ SEQUENCE 477 AA; 51967 MW; 0301F8F0D8D4BD88 CRC64; MQAKPTTAVK QKQNFGQRLF TLLRNRDFMI SFLITVVLLV LFRVLAIIPL PGIQVNQTGL DQNSNDFFSL FNLLGGGGLN QLSLFAVGIS PYISAQIVMQ LLSTDLIPPL SKLVNSGEVG RRKIEMITRI ITLPFALVQS FAVIQIATNS GGGSSPITLK NNGSDFVAFY IIAMTAGTYL SVFLGDTISK KGIGNGITLL ILSGILAQLP EGFIAAYSVL SGVVVTINAT LTTAISFFIY FMAFVTLLFA TTFITQETRK IPIQQSGQGL VTESSALPYL PIKVNSAGVI PVIFASSIMS IPVTIAQFQP QTESRWFVED YLSLSKPTGI VLYGILVILF SFFYSYIQIN PERLAKNFEK SGRFIPGIRP GKDTEKHIAR VLVRINFIGA PFLTVIAIIP YIVSALIHLP NSLSLGGTGI IIIVTAVVEF MSALRSAATA TNYQQLRRNL AIEVQKTAQQ DKEEQLRAET PGIGNLW //