SECD_SYNFM
ID SECD_SYNFM Reviewed; 533 AA.
AC A0LHM9;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=Sfum_1239;
OS Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC Syntrophobacteraceae; Syntrophobacter.
OX NCBI_TaxID=335543;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10017 / MPOB;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J.,
RA Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL Submitted (OCT-2006) 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:0000255|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:0000255|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01463}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
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DR EMBL; CP000478; ABK16931.1; -; Genomic_DNA.
DR RefSeq; WP_011698102.1; NC_008554.1.
DR AlphaFoldDB; A0LHM9; -.
DR SMR; A0LHM9; -.
DR STRING; 335543.Sfum_1239; -.
DR EnsemblBacteria; ABK16931; ABK16931; Sfum_1239.
DR KEGG; sfu:Sfum_1239; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_7; -.
DR OMA; MVVYYRL; -.
DR OrthoDB; 121331at2; -.
DR Proteomes; UP000001784; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 HAMAP; MF_01463_B; SecD_B; 1.
DR InterPro; IPR005791; SecD.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR022646; SecD/SecF_CS.
DR PANTHER; PTHR30081; PTHR30081; 2.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR01129; secD; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..533
FT /note="Protein translocase subunit SecD"
FT /id="PRO_5000166173"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 400..420
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ SEQUENCE 533 AA; 57931 MW; 54FA7845143256E9 CRC64;
MSNLKWRALL VVVVLIVGVV YLVPTFVSTL PPGWSKFLPK DKIRLGLDLQ GGMHLILEVE
ADQAVSNTAT RLAEDLKDAF RKEKIAFNKI DKTGKWDIEV QLPGTEQQSQ IGPLVEKEFP
TLKWVSAETQ PEGTVKVMLT VHEKEVERVQ KAAIAQGLET IRNRIDQFGV SEPDIRPQGE
DRILVQLPGI QDPQRAVELI GKTAQLEFKL VAEGVSPQDV KSGKAPAGTK IYPMKHTDRT
TRQRTESQIV LNDRTLMSGE YITNAQVEID RQHSSSYVAL DFDAQGAKLF EKITEANVKK
QLAIVLDGVV YSAPVIQETI GGGKATITGS FTDQEARDLA IVLRAGALPA PVKILEQRTV
GPSLGADSIN KGVLASIVGG IGTILFMLIY YRFGGVVADL ALALNVLLVL AGMAAFGFTL
TLPGIAGIAL TIGMAVDANV LIYERIREEL RLGKTPRAAL ETGYDRATLT ILDANVTTII
AALVLLQFGT GPVRGFAVTL TVGLAANMFT AIFVTRVIFD YLLVQRRIKT LSI
