ID F7RJW5_9GAMM Unreviewed; 604 AA.
AC F7RJW5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=SOHN41_00921 {ECO:0000313|EMBL:EGM71187.1};
OS Shewanella sp. HN-41.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM71187.1, ECO:0000313|Proteomes:UP000002956};
RN [1] {ECO:0000313|EMBL:EGM71187.1, ECO:0000313|Proteomes:UP000002956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-41 {ECO:0000313|EMBL:EGM71187.1,
RC ECO:0000313|Proteomes:UP000002956};
RX PubMed=21868804; DOI=10.1128/JB.05578-11;
RA Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA Hur H.G.;
RT "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT Arsenic-Sulfide Nanotubes.";
RL J. Bacteriol. 193:5039-5040(2011).
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:EGM71187.1}.
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DR EMBL; AFOZ01000014; EGM71187.1; -; Genomic_DNA.
DR RefSeq; WP_007646014.1; NZ_AFOZ01000014.1.
DR AlphaFoldDB; F7RJW5; -.
DR STRING; 327275.SOHN41_00921; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000002956; 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; 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:SF13; 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 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 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 442..461
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 468..490
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 496..514
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 535..560
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 566..590
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 10..100
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 232..290
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 422..592
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 604 AA; 65606 MW; 32F67BF60E62FC0A CRC64;
MEIKPNQRLL NHYSAWKYIV LIVTIIVMLF SALPTFYGED AAVQVGAKAG LTLTPVALRD
KLQAEGVTVK RIDQKNGETL IVLDADNQQT LVKTFVSSMV ADPKELTLSL ASAAPSWLQN
LGFQPIKLGL DLRGGVQFLL DVDVDPVYQT QGEALVDSLR QFIREQKIRG ASVYLDQASQ
LNLTLPDNDA RAAVRQMMKQ SYPNWQLSNT DGAGLQIKLS PEEQTKLRNL TVQQNLQVMR
SRIEELGITE ALVQRQGDHR IRIELPGVQD PAAAKNVIGA TASLAFFEVK ESGSVNAMVL
NDKSGKPIYV SRTPVLGGDH IVDARASLGE MGMAEVNINL DRVGGQKMSE FSRTNIGKPM
ATSYSEYSRD EQGKAKQTQE IISVATIQSQ LGDRFRITGA GTYQEAQQLA LLLRAGSMTA
PVTIVEERTI GPTLGAENIE NGFAALGLGM GITLLFMALW YRRLGWVANI ALISNMVILF
GLLALIPGAV LTLPGIAGLV LTVGMAVDTN VLIFERIKDK LKEGRSFALA IDTGFDSAFS
TIFDANFTTM ITAVVLYSIG NGPIQGFALT LGLGLLTSMF TGIFASRALI NLVYGRDASR
HVRV
//
