ID A0A1E7R2X2_9GAMM Unreviewed; 450 AA.
AC A0A1E7R2X2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:KAA8733937.1};
GN ORFNames=BJI46_04275 {ECO:0000313|EMBL:OEY93666.1}, F4V57_07155
GN {ECO:0000313|EMBL:KAA8733937.1};
OS Acinetobacter qingfengensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1262585 {ECO:0000313|EMBL:OEY93666.1, ECO:0000313|Proteomes:UP000185895};
RN [1] {ECO:0000313|EMBL:OEY93666.1, ECO:0000313|Proteomes:UP000185895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANC 4671 {ECO:0000313|EMBL:OEY93666.1,
RC ECO:0000313|Proteomes:UP000185895};
RA Capua I., De Benedictis P., Joannis T., Lombin L.H., Cattoli G.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAA8733937.1, ECO:0000313|Proteomes:UP000323633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 69710T {ECO:0000313|EMBL:KAA8733937.1,
RC ECO:0000313|Proteomes:UP000323633};
RA Pineiro-Iglesias B., Tunovic T., Unosson C., Inganas E., Ohlen M.,
RA Cardew S., Jensie-Markopoulos S., Salva-Serra F., Jaen-Luchoro D.,
RA Karlsson R., Svensson-Stadler L., Chun J., Moore E.;
RT "Draft genome sequence of various Type strains from the CCUG.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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:OEY93666.1}.
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DR EMBL; VXKN01000004; KAA8733937.1; -; Genomic_DNA.
DR EMBL; MKKK01000045; OEY93666.1; -; Genomic_DNA.
DR RefSeq; WP_070070480.1; NZ_VXKN01000004.1.
DR AlphaFoldDB; A0A1E7R2X2; -.
DR STRING; 1262585.BJI46_04275; -.
DR OrthoDB; 9809248at2; -.
DR Proteomes; UP000185895; Unassembled WGS sequence.
DR Proteomes; UP000323633; 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 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.
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:UP000185895};
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 28..46
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 82..107
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 128..149
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 155..175
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 187..205
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 272..295
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 322..344
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 379..397
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT TRANSMEM 403..424
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
SQ SEQUENCE 450 AA; 49005 MW; 14ACD1D968A9662B CRC64;
MSPGSSGHVH MQKGQPFYVK YREIIRRLMF LIGALLVFRL GAHIPVPGIN NAALDRLFNA
NQGTILGLFN MFSGGALERM SILALGIMPY ISASIIVQLM STVVPSLEAL KKEGEQGKRK
INQYTRQGTL LLAFVQAMGM CAGLISQGIT LSTGLGFYVP AVTSLVAGTM FLMWLGEQIT
ERGVGNGISM IIFAGIVATL PTHAMQTFSA IENGQSTLIG VLVLIVITIA VMAAIIFIEK
AQRRVPVNYA QKQQGRRIFT AQQTHLPLKI NMAGVIPAIF ASSLLLFPAS LGHWIGSSDA
NASFFKRSLQ DLALVLSPGQ PLYLVLFGSL IIFFCYFYTA LVFSPKEVAE NLKRSGAYVP
GIRPGEQTAR YLDHILNRLT FIGAIYITIV CLMPMVLQTS FGVQFNLGGT SLLIVVVVVM
DFMAQLQAHL TSHQYDNQSL MKKSTAHPKG
//
