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Database: UniProt
Entry: A0A1H2S740_9BACI
LinkDB: A0A1H2S740_9BACI
Original site: A0A1H2S740_9BACI 
ID   A0A1H2S740_9BACI        Unreviewed;       433 AA.
AC   A0A1H2S740;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=SAMN05421781_1062 {ECO:0000313|EMBL:SDW27502.1};
OS   Marinococcus luteus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Marinococcus.
OX   NCBI_TaxID=1122204 {ECO:0000313|EMBL:SDW27502.1, ECO:0000313|Proteomes:UP000199488};
RN   [1] {ECO:0000313|EMBL:SDW27502.1, ECO:0000313|Proteomes:UP000199488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23126 {ECO:0000313|EMBL:SDW27502.1,
RC   ECO:0000313|Proteomes:UP000199488};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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. Other proteins may also be involved.
CC       {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}.
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DR   EMBL; FNNC01000001; SDW27502.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2S740; -.
DR   STRING; 1122204.SAMN05421781_1062; -.
DR   Proteomes; UP000199488; 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; 3.30.70.3220; -; 1.
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; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199488};
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..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        261..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        310..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        355..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        383..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          63..121
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          239..401
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   433 AA;  47763 MW;  0FBA7E58C7758931 CRC64;
     MVKKSRIVYF FLIIFALAAL MIPTSEKIVN GIDLGLDLQG GFEVLYEVEP QEEGQEITDE
     TLQNTVAALT QRVDILGVSE PNITIEGEDR IRVQLAGVED QQSARELLST EANLSIRDVD
     DNERLSGSDI QENSASVNFD DSNNPIVTVS LRDGDQFGEV TENIINEYQP PDNRLVIWLD
     YEEGDSYEEE ATKEDPKFIS APAVDEPLYT QDIQIEGDFS VEEAENIADI LNSGSLPVDL
     EEVYSNSVGA SLGEQAMDKT IFATIIGVGL IFLFMLVFYR FTGFIAVLTL STYIYFVLAV
     FNFIQGVLTL PGIAALVLGV GMAVDANIIT YERIKEEIKY GRSILSAYRS GARRSLGTII
     DANVTTLIAA GVLFYFGTSS VQGFALMLIV SILVSFITAV LGTRLLLGLW VNSRIFNKKP
     KVFGVKERDI HEP
//
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