ID F5YXU7_MYCSD Unreviewed; 443 AA.
AC F5YXU7;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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 ECO:0000313|EMBL:AEF37301.1};
GN OrderedLocusNames=JDM601_3301 {ECO:0000313|EMBL:AEF37301.1};
OS Mycolicibacter sinensis (strain JDM601) (Mycobacterium sinense).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacter.
OX NCBI_TaxID=875328 {ECO:0000313|EMBL:AEF37301.1, ECO:0000313|Proteomes:UP000009224};
RN [1] {ECO:0000313|EMBL:AEF37301.1, ECO:0000313|Proteomes:UP000009224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDM601 {ECO:0000313|EMBL:AEF37301.1,
RC ECO:0000313|Proteomes:UP000009224};
RX PubMed=21685274; DOI=10.1128/JB.05291-11;
RA Zhang Z.Y., Sun Z.Q., Wang Z.L., Wen Z.L., Sun Q.W., Zhu Z.Q., Song Y.Z.,
RA Zhao J.W., Wang H.H., Zhang S.L., Guo X.K.;
RT "Complete genome sequence of a novel clinical isolate, the nontuberculous
RT Mycobacterium strain JDM601.";
RL J. Bacteriol. 193:4300-4301(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, 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; CP002329; AEF37301.1; -; Genomic_DNA.
DR RefSeq; WP_013830228.1; NC_015576.1.
DR AlphaFoldDB; F5YXU7; -.
DR STRING; 875328.JDM601_3301; -.
DR KEGG; mjd:JDM601_3301; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_0_11; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000009224; 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:UP000009224};
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 18..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 70..97
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 118..139
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 159..180
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 187..206
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 218..237
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 265..286
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 320..342
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 374..396
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 408..426
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 443 AA; 48262 MW; 7B5D432392ACCD96 CRC64;
MFSAFISSLR TVDLRRKILF ALGIIIIYRL GAAIPSPGVD YQNVQQCIKE VSGGDAAQVY
SLINLFSGGA LLQLTVFAIG VMPYITASII VQLLTVVIPR FEELRKEGQS GQNKMTQYTR
YLTVALAVLQ ATSIVALAAN GGLLQTCSLR HDIIADHSIF TLVVIVMVMT AGAVLVMWLG
ELITERGIGN GMSLLIFVGI AARIPIEGKT ILDSRGGLVF TMVCLAALVI VVGVVFVEQG
QRRIPVQYAK RMVGRRMYGG TSTYLPLKVN QAGVIPVIFA SSLIYIPQLV TQLVRSGSGG
VGNSWWDKAV STYLSDPSNL VYIAVYFGLI IFFTYFYVSI TFNPDERADE MKKFGGFIPG
IRPGRPTADY LRFVLNRITL PGSIYLGVIS VLPNLFLQMG NSGTVQNLPF GGTAVLIMIG
VGLDTVKQIE SQLMQRNYEG FLK
//
