ID A0A0F7CU94_9CHLR Unreviewed; 448 AA.
AC A0A0F7CU94;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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:AKG54280.1};
GN ORFNames=DGWBC_1654 {ECO:0000313|EMBL:AKG54280.1};
OS Dehalogenimonas sp. WBC-2.
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalogenimonas.
OX NCBI_TaxID=943347 {ECO:0000313|EMBL:AKG54280.1, ECO:0000313|Proteomes:UP000034106};
RN [1] {ECO:0000313|EMBL:AKG54280.1, ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|EMBL:AKG54280.1,
RC ECO:0000313|Proteomes:UP000034106};
RX PubMed=26452554; DOI=10.1128/AEM.02017-15;
RA Molenda O., Quaile A.T., Edwards E.A.;
RT "Dehalogenimonas sp. Strain WBC-2 Genome and Identification of Its trans-
RT Dichloroethene Reductive Dehalogenase, TdrA.";
RL Appl. Environ. Microbiol. 82:40-50(2015).
RN [2] {ECO:0000313|Proteomes:UP000034106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WBC-2 {ECO:0000313|Proteomes:UP000034106};
RA Molenda O., Edwards E.A.;
RT "Identification of trans-1,2-dichloroethene reductive dehalogenase (TdrA)
RT in Dehalogenimonas sp. WBC-2.";
RL Submitted (MAY-2015) 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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR EMBL; CP011392; AKG54280.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7CU94; -.
DR STRING; 943347.DGWBC_1654; -.
DR KEGG; dew:DGWBC_1654; -.
DR PATRIC; fig|943347.4.peg.1696; -.
DR Proteomes; UP000034106; Chromosome.
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; -; 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; 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; 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 271..290
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 297..316
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 376..395
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 401..424
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 69..121
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 253..427
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 448 AA; 47740 MW; BBCC62FD1F70E8A0 CRC64;
MKKHLPGLIT IFVLLILSAL IVLPMGKGVL FGKPISLGLD LQGGIHLVYQ ADLSGVAEAD
KDATIEGILG VINNRINPLG VSEPSIYRQG EDRIVVELPG TSLSDAQKQR IGSTALLIFG
ELAADDEEAT WENDLGRWKP ATAEIDGVVL ELDSSYFNEN TYVTTDQFGS IQLHFEWNAE
GTKIFESVTS RLVGKRIGLF EGDTALLGDD GNPIAPVVQQ ALSDSGVITG LSTHEAQLLS
QQLNAGRLPV PLEVIYENTV SPILGADFVD LSVLAGVIGF ILVIIFMTIF YRLPGALASL
ALVIYVALVL AIYKLVPVTL TLAGIGGFIL SIGMAVDANV LIFERMKEEL RSRRTVGAAI
EAGFSRAWSA IWDANVTTLI VCAILVWVGG SVAAGAPVQG FALTLGIGVL ASMFTAIFIT
RTFLRALIGS SISKKLNLFT TETGDQNA
//
