ID A0A5M8FGU1_9GAMM Unreviewed; 618 AA.
AC A0A5M8FGU1;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463,
GN ECO:0000313|EMBL:KAA6183634.1};
GN ORFNames=F2Q65_15015 {ECO:0000313|EMBL:KAA6183634.1};
OS Thiohalocapsa marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thiohalocapsa.
OX NCBI_TaxID=424902 {ECO:0000313|EMBL:KAA6183634.1, ECO:0000313|Proteomes:UP000322981};
RN [1] {ECO:0000313|EMBL:KAA6183634.1, ECO:0000313|Proteomes:UP000322981}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19078 {ECO:0000313|EMBL:KAA6183634.1,
RC ECO:0000313|Proteomes:UP000322981};
RA Kyndt J.A., Meyer T.E.;
RT "Whole-genome sequence of the purple sulfur bacterium Thiohalocapsa marina
RT DSM 19078.";
RL Submitted (SEP-2019) 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-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:KAA6183634.1}.
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DR EMBL; VWXX01000030; KAA6183634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5M8FGU1; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000322981; 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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000322981};
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 457..478
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 485..503
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 509..531
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 552..573
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 585..608
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 1..103
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 229..287
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 437..604
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 618 AA; 67617 MW; 7025F957393FA05F CRC64;
MNHYPLWKNL LILVVILVGL LFALPNLFSQ DPSIEVAGTR DNPVTEASIA EIAAAMENAG
VPVKAVEPRE GEKLLVRFTT PSEQLRGQEV LDQVLSDRYA NALTTAPDLP GWLEGLGAQP
MFLGLDLRGG IHVLIDVDME AAVDQALERY VGDFRTELRK EKVRYITVTR DGGRLAVRFK
DEQARDQAED ILRKAFRDLT LETGEEAGQY YVYAVLPQAI QQQIKTFALQ QNITTLRNRV
NALGVAEPII QRQGERRIVV QLPGASDPAR LKELLGATAT LEYRLVDTEN DVQDALEGRV
PVGSALYRER DGRPILLKRR VIVTGDQITD ASAGFDQQSG SPAVFVNLDG QGARRMRSIT
TENVGKPMAV VFIENRTITR MVDGEPVKER VRTEEVISVA NILEPFGRRF QTTGLDSSDE
AHNLALLLRA GALAAPIEIV EERTIGPSLG QDNIDQGFRS VIIGLVLVMV FMALYYRVFG
LVADLVLVIN LVMMVAVLSM LQATLTLPGI AGIVLTVGMA VDANVLIFER IREEIRNGSS
PQASIHAGYD KALSTIVDAN ITTLIAAIVL FSFGTGPVKG FAVTLFIGIV TSMFTAILGS
RALINLIYGG RRLKRLAI
//
