ID F8C740_MYXFH Unreviewed; 590 AA.
AC F8C740;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN OrderedLocusNames=LILAB_31400 {ECO:0000313|EMBL:AEI68161.1};
OS Myxococcus fulvus (strain ATCC BAA-855 / HW-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=483219 {ECO:0000313|EMBL:AEI68161.1, ECO:0000313|Proteomes:UP000000488};
RN [1] {ECO:0000313|EMBL:AEI68161.1, ECO:0000313|Proteomes:UP000000488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-855 / HW-1 {ECO:0000313|Proteomes:UP000000488};
RX PubMed=21868801; DOI=10.1128/JB.05516-11;
RA Li Z.F., Li X., Liu H., Liu X., Han K., Wu Z.H., Hu W., Li F.F., Li Y.Z.;
RT "Genome sequence of the halotolerant marine bacterium Myxococcus fulvus HW-
RT 1.";
RL J. Bacteriol. 193:5015-5016(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. Other proteins may also be involved.
CC {ECO:0000256|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01463}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002830; AEI68161.1; -; Genomic_DNA.
DR AlphaFoldDB; F8C740; -.
DR STRING; 483219.LILAB_31400; -.
DR KEGG; mfu:LILAB_31400; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_7; -.
DR Proteomes; UP000000488; 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; 3.30.70.3220; -; 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; 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 SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
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 9..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 429..448
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 524..546
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 552..576
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 166..225
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 411..579
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 590 AA; 64408 MW; D17C6B04FB22940D CRC64;
MDRGWWWKFG LIVAVTLGSI WFLIPTYYSL VVLDRDQRNN LAVLEERMPS WAPPAKYRLN
LGLDLQGGIH MVMRVDTKTA LQKRTERRAQ QIVNYVNDKK LGEVTADTDP EKLEVTLTAK
DPATMDAIQK EVLATFTDFK EVSRSGAALT LVQDESQANV FRTEAVDQAM LVIRRRIDKW
GVAEVDVRKL GSDSIQISLP GRSNPEQAKE LVGTTAQLEF RMVDDSNPQF FAQLLQATPP
PEGSDITLTT EGGFPQLQAP TREAIIRYTQ DKVPENRVVL TECIANPVKK NECTSYRSYL
LDRNVPLTGE SLAGADANIS QLNEPEVNIS FDPAGAREFE RLTEAGVGRR MAIVLDDNVQ
TAPNINEKIS GGSARITMGR MGGRTFEEWL GEAQTLALVL KAGALPAPVT VGEIRQVGAS
LGDELIRKGG LAAVLGLGLV VLFMALYYKA AGLIADVSLL LNGLLILAGL AFFNATLTLP
GIAGFVLTLG VAVDANVLIN ERIREELGHG KSARAAVDQG YDRAFWTIFD SHVTALISAF
ILFFTGTGPV RGFATTLIIG LLASLFTSIT VTRVIMTYFV HGRNAKVVSV
//
