ID R1F5Y1_9GAMM Unreviewed; 617 AA.
AC R1F5Y1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=G113_09997 {ECO:0000313|EMBL:EOD55243.1};
OS Aeromonas molluscorum 848.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1268236 {ECO:0000313|EMBL:EOD55243.1, ECO:0000313|Proteomes:UP000013526};
RN [1] {ECO:0000313|EMBL:EOD55243.1, ECO:0000313|Proteomes:UP000013526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=848 {ECO:0000313|EMBL:EOD55243.1,
RC ECO:0000313|Proteomes:UP000013526};
RX PubMed=23788549;
RA Spataro N., Farfan M., Albarral V., Sanglas A., Loren J.G., Fuste M.C.,
RA Bosch E.;
RT "Draft Genome Sequence of Aeromonas molluscorum Strain 848TT, Isolated from
RT Bivalve Molluscs.";
RL Genome Announc. 1:E00382-13(2013).
CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC the SecYEG preprotein conducting channel. SecDF uses the proton motive
CC force (PMF) to complete protein translocation after the ATP-dependent
CC function of SecA. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec protein
CC translocation apparatus which comprises SecA, SecYEG and auxiliary
CC proteins SecDF-YajC and YidC. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01463}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01463}.
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:EOD55243.1}.
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DR EMBL; AQGQ01000055; EOD55243.1; -; Genomic_DNA.
DR RefSeq; WP_005899991.1; NZ_AQGQ01000055.1.
DR AlphaFoldDB; R1F5Y1; -.
DR PATRIC; fig|1268236.3.peg.1978; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000013526; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
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; 3.30.1360.200; -; 1.
DR Gene3D; 3.30.70.3400; -; 2.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR HAMAP; MF_01463_B; SecD_B; 1.
DR InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR005791; SecD.
DR InterPro; IPR027398; SecD-TM.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR022646; SecD/SecF_CS.
DR InterPro; IPR048631; SecD_1st.
DR InterPro; IPR048634; SecD_SecF_C.
DR NCBIfam; TIGR00916; 2A0604s01; 1.
DR NCBIfam; TIGR01129; secD; 1.
DR PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF13721; SecD-TM1; 1.
DR Pfam; PF21760; SecD_1st; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01463};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01463};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01463}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 505..527
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 560..577
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 583..607
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 2..103
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 229..288
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 435..596
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 617 AA; 67286 MW; 21D76882C5F0AFFE CRC64;
MLNRYPLWKY LMVIIVIAIG FLYAAPNLYG EDPALQVSAS RGAEVQLKTL DQVKAILDEA
AIPVKHAAFE HDQILVRFTN TEDQLKARDL VASKLGDNFV TALNLAPSTP AWLEAIGANP
LKLGLDLRGG VHFLMEVDMA EALVKQQDQM VQDFRTELRT QKIRYSGVRR AGDRVEILFR
DEADQEKAIA HLRRLNADLT FNSEQKGNDF LILASLSEAK IKEVKKYALE QNITIIRNRV
NELGVAEPLV QQQGAERIVV ELPGIQDTAR AKEILGATAT LEFHMVDETA DPQAAADGRV
PPSSKVYTDR NGRPVVLQKR IILTGDHIVG AQSGFDEYSR PQVNIKLDGQ GGNKMANFTK
DNVGKGMATV FIEYKPVGEP GPDGKRKFRK QEEVINVATI QSRLGSQFRI TGIDNANEAH
NLALLLRAGA LIAPIQIVEE RTIGPSLGQQ NIDSGLQAMG YGMLAIVIFM ALYYRKFGLV
ANLALVVNVV LIIGLMSMIP GATMTLPGIA GIVLTMGMAV DANVLIFERI REELRAGRGV
QQAINLGYEK AFGTIADSNI TTLITCIILF AVGTGAIKGF ALTLAIGILA SMFTAITGTR
AIVNLAWGGK RLDKLPI
//
