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Database: UniProt
Entry: N9TZE1_9GAMM
LinkDB: N9TZE1_9GAMM
Original site: N9TZE1_9GAMM 
ID   N9TZE1_9GAMM            Unreviewed;       614 AA.
AC   N9TZE1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=G114_12704 {ECO:0000313|EMBL:ENY71494.1};
OS   Aeromonas diversa CDC 2478-85.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=1268237 {ECO:0000313|EMBL:ENY71494.1, ECO:0000313|Proteomes:UP000023775};
RN   [1] {ECO:0000313|EMBL:ENY71494.1, ECO:0000313|Proteomes:UP000023775}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2478-85 {ECO:0000313|EMBL:ENY71494.1,
RC   ECO:0000313|Proteomes:UP000023775};
RX   PubMed=23792745; DOI=10.1128/genomeA.00330-13;
RA   Farfan M., Spataro N., Sanglas A., Albarral V., Loren J.G., Bosch E.,
RA   Fuste M.C.;
RT   "Draft Genome Sequence of the Aeromonas diversa Type Strain.";
RL   Genome Announc. 1:S69-S82(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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:ENY71494.1}.
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DR   EMBL; APVG01000033; ENY71494.1; -; Genomic_DNA.
DR   RefSeq; WP_005355488.1; NZ_CDCE01000029.1.
DR   AlphaFoldDB; N9TZE1; -.
DR   PATRIC; fig|1268237.3.peg.2501; -.
DR   eggNOG; COG0342; Bacteria.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000023775; 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        452..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        478..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        548..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        576..600
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          432..600
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   614 AA;  67008 MW;  663458A0AF81E97E CRC64;
     MLNRFPLWKN LMVILVIAIG FLYAAPNLYG EDPALQVSAS RGAEVQLSTL EQVKGIIDEA
     GIPIKHAAFE QGQILIRFTN TEAQLKARDL VAAKLGDDFV VALNLAPSTP AWLESVGAAP
     LKLGLDLRGG VHFLMEVDMD EAIAKQQEQM VQDFRSELRN QKIRYSGVNR GGDQVLVRFR
     DQESLDKAVS HLRRLNPDIT FNKESADGQF VLRAAMSEQK LKEVRKYALE QNITIIRNRV
     NELGVAEPLV QQQGADRIVV ELPGIQDTAR AKEILGATAT LEFHMVDETA DAQSGRVPPS
     SKLYADRNGR PVVLQKRIIL TGDHIVGAQS GFDEYSRPQV NIKLDGQGGN KMAAFTKDNV
     GKGMATVFIE YKPVGEPGPD GKRKFRKNEE VINVATIQSR LGSQFRITGI DNANEAHNLA
     LLLRAGALIA PIQIVEERTI GPSLGQQNID SGLQAMMWSM VVIVLFMGIY YRTFGWVANL
     ALCLNLVLLV GVMSMIPGAT MTLPGIAGIV LTLGMAIDAN VLIYERIREE LRAGRGVQQA
     IHLGFDRAFS TIADSNITSL ITAVILFGIG TGPIKGFALT LGIGLTISMF TAITVSRAII
     NLGWGGRRLD KLPI
//
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