ID E1VKD8_9GAMM Unreviewed; 841 AA.
AC E1VKD8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01463, ECO:0000256|HAMAP-Rule:MF_01464};
DE Includes:
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
DE Includes:
DE RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463,
GN ECO:0000313|EMBL:CBL45280.1};
GN Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN ORFNames=HDN1F_16970 {ECO:0000313|EMBL:CBL45280.1};
OS gamma proteobacterium HdN1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL45280.1, ECO:0000313|Proteomes:UP000002677};
RN [1] {ECO:0000313|EMBL:CBL45280.1, ECO:0000313|Proteomes:UP000002677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT "Alkane degradation by a new type of denitrifying bacterium with possible
RT involvement of the electron acceptor in substrate activation.";
RL Environ. Microbiol. 0:0-0(2010).
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 SecD. 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_01464}.
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 -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01464}.
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; FP929140; CBL45280.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VKD8; -.
DR STRING; 83406.HDN1F_16970; -.
DR KEGG; gpb:HDN1F_16970; -.
DR eggNOG; COG0341; Bacteria.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_3_0_6; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000002677; 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; -; 2.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR HAMAP; MF_01463_B; SecD_B; 1.
DR HAMAP; MF_01464_B; SecF_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 InterPro; IPR005665; SecF_bac.
DR NCBIfam; TIGR00916; 2A0604s01; 2.
DR NCBIfam; TIGR01129; secD; 1.
DR NCBIfam; TIGR00966; transloc_SecF; 1.
DR PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF07549; Sec_GG; 2.
DR Pfam; PF21760; SecD_1st; 1.
DR Pfam; PF02355; SecD_SecF; 2.
DR PRINTS; PR01755; SECFTRNLCASE.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
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:UP000002677};
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..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 351..372
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 450..472
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 478..501
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 534..557
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 659..677
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 709..726
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 764..786
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 792..814
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 154..211
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 336..499
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 630..816
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 841 AA; 90082 MW; 1DC4E2F4AB7D1862 CRC64;
MRQFRARIWI YSIVILIGLL SAVPNFLTPE LASKLPEGLA QNKIVLGLDL RGGSHLLLEV
ETPALSADRM YQNAEVISSE LRKAGISHLR PAKTQDSAKI TLKNASDFEK AAGIARSKAK
QNGVIQFTVE QQGTSMALVP TPEMILGLKQ DAAERSIDVL RRRLDETGVV DPTITRQGAD
SILVQLPGVS NPAHIRELLG KTARLTFHLV VEEGERSRGG AMTLPSQQGD SVRLEQRTLL
DGAHLADARL GYNQNTGEPL VNFHLDAIGA KRFAKITKES IGRALAVVLD GRVITAPVIR
GVIGGGSGEI TGGFTVTEAK DLALLLRAGA LPAPLKVIEE RTVGPDLGSD AIQMGVTTGL
LGMALVFIFI VTLYGRWGVI ADVALALNIG LSVGVLSAFG ATLTLPGIAG LILSIGMAVD
ANILINERIR EEVNKTHNAL DALAAGFDRA YATIIDSNLT TLIAISLLFL FGSGPIKGFA
VAMAVGLVVS LFTAISVTRL LMEWRVRRGN HTSISMKGLL PLERIQPDKP IKFLNARVAG
LTFSAVLSAA SIALMFYPGL SKGIDFQGGN VIELRTNPQI SVEKLRAAFQ QAGLKEIAIQ
EFGAPGSFMV RSPLVSSEDA ASGGVVDQIK EVVLKEDPHA EFPRVEIVGP KVSGSFADTS
VLALLLAGGG MFVYLWIRFE FHFAIAALAT LVLDMTKMLG FFALTGVEFN LSAVAALLAL
IGYSVNDKVV VFDRIREFLR KGQRNIDLKE LMDLSITSTL TRTIFTSVTT FLCLLPMGIA
GGAAVSSFAL PMLFGIVLGT SSSIFIAAPI LYLLGERRIR MGLGQIDMGE TEEEEKRQSY
P
//
