ID A0A0D6XPT7_9STAP Unreviewed; 402 AA.
AC A0A0D6XPT7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Accessory Sec system protein translocase subunit SecY2 {ECO:0000256|HAMAP-Rule:MF_01466};
GN Name=secY {ECO:0000313|EMBL:KIX90251.1};
GN Synonyms=secY2 {ECO:0000256|HAMAP-Rule:MF_01466};
GN ORFNames=TP70_08690 {ECO:0000313|EMBL:KIX90251.1};
OS Staphylococcus microti.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=569857 {ECO:0000313|EMBL:KIX90251.1, ECO:0000313|Proteomes:UP000032366};
RN [1] {ECO:0000313|EMBL:KIX90251.1, ECO:0000313|Proteomes:UP000032366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22147 {ECO:0000313|EMBL:KIX90251.1,
RC ECO:0000313|Proteomes:UP000032366};
RA Guo J.;
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of the accessory SecA2/SecY2 system specifically
CC required for export of possible cell wall proteins. The central subunit
CC of a protein translocation channel. {ECO:0000256|HAMAP-Rule:MF_01466}.
CC -!- SUBUNIT: Component of the accessory SecA2/SecY2 protein translocase
CC complex required to export cell wall proteins. May form heterotrimers
CC with SecE and SecG subunits. {ECO:0000256|HAMAP-Rule:MF_01466}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01466};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01466}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. SecY2 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01466}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01466}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIX90251.1}.
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DR EMBL; JXWY01000066; KIX90251.1; -; Genomic_DNA.
DR RefSeq; WP_044361039.1; NZ_UHDT01000001.1.
DR AlphaFoldDB; A0A0D6XPT7; -.
DR STRING; 569857.TP70_08690; -.
DR PATRIC; fig|569857.6.peg.2224; -.
DR OrthoDB; 2055747at2; -.
DR Proteomes; UP000032366; Unassembled WGS sequence.
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 Gene3D; 1.10.3370.10; SecY subunit domain; 1.
DR HAMAP; MF_01466; SecY2; 1.
DR InterPro; IPR002208; SecY/SEC61-alpha.
DR InterPro; IPR014269; SecY2.
DR InterPro; IPR023201; SecY_dom_sf.
DR NCBIfam; TIGR02920; acc_sec_Y2; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR PRINTS; PR00303; SECYTRNLCASE.
DR SUPFAM; SSF103491; Preprotein translocase SecY subunit; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01466};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01466};
KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01466};
KW Translocation {ECO:0000256|HAMAP-Rule:MF_01466};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_01466};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01466};
KW Transport {ECO:0000256|HAMAP-Rule:MF_01466}.
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01466"
FT TRANSMEM 105..125
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01466"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01466"
FT TRANSMEM 157..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01466"
FT TRANSMEM 187..209
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01466"
FT TRANSMEM 283..300
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01466"
FT TRANSMEM 335..358
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01466"
FT TRANSMEM 364..382
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01466"
SQ SEQUENCE 402 AA; 46437 MW; 4133AE97A4654B0F CRC64;
MNRILRQYEY KVLYKRCAFT FLILFIYILG SRITIVDPSH MIVKDKSFYQ LAVSNVGGDI
QTLNLFSLGL GPWLTALIFL MLVRYRDVEK SAQLTRREKH YQEKLLALML SVVQGYFVIY
QYVSVQQREH TNIWLMLLIL VAGTMLLIWL ADQNVRYGIA GAMPIVLMSI IRSIFHQQLP
DVAIDGWLLT LIVVLIGVTL VILLFMEFVE YRLHYRDIMQ VDQSRAQTFV AWKINPAGSI
SIMISLSVFI LLNSLLNMIF NFLPDLSVDL DVLQLSHPVG VTVYILLQVT LGYALSRLLI
HTKQTSKTFL KSGNYFEKIQ PGPETNRYLN HKARLVCWTG AGIVGVIIGV PMYLSLLVPQ
LSQQIYFAIQ LMIVMYISIN IAETVRTYLY FDKYQQFLTK YW
//
