ID A0A0G0JP38_9BACT Unreviewed; 1064 AA.
AC A0A0G0JP38;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=secDF {ECO:0000313|EMBL:KKQ69328.1};
GN Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463}, secF
GN {ECO:0000256|HAMAP-Rule:MF_01464};
GN ORFNames=US89_C0002G0108 {ECO:0000313|EMBL:KKQ69328.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_38_29.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619066 {ECO:0000313|EMBL:KKQ69328.1, ECO:0000313|Proteomes:UP000033957};
RN [1] {ECO:0000313|EMBL:KKQ69328.1, ECO:0000313|Proteomes:UP000033957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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. Other proteins may also be involved.
CC {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. 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 -!- 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}.
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:KKQ69328.1}.
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DR EMBL; LBUS01000002; KKQ69328.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0JP38; -.
DR STRING; 1619066.US89_C0002G0108; -.
DR PATRIC; fig|1619066.4.peg.176; -.
DR Proteomes; UP000033957; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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; 3.10.50.40; -; 1.
DR Gene3D; 3.30.1360.200; -; 1.
DR Gene3D; 3.30.70.3220; -; 1.
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; IPR004869; MMPL_dom.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
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 InterPro; IPR000731; SSD.
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; PF03176; MMPL; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR Pfam; PF07549; Sec_GG; 2.
DR Pfam; PF21760; SecD_1st; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR01755; SECFTRNLCASE.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 3.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
DR PROSITE; PS50156; SSD; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01463}; Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
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}; Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
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 524..541
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 547..566
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 573..593
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 599..621
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 733..754
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 888..907
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 919..945
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 951..972
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 1007..1029
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 1035..1054
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 247..357
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
FT DOMAIN 888..1052
FT /note="SSD"
FT /evidence="ECO:0000259|PROSITE:PS50156"
SQ SEQUENCE 1064 AA; 117019 MW; AF5511BBE18CC051 CRC64;
MKRTVWQIAI IILFAVFLGL YNAPASVQKA LHLPDSITKD KIHLGLDLQG GSQLDYKVDL
RKVPAKDQAA IVDGVLQVIT KRVNGLGVSE PSIYTSNVGD EQHIIVELAG IKDLEEAKKV
VGKTIQLEFK EQKEKADPQE VERMKEYAQN VLKNILKKND ITLAGKEEEQ NNIGKVKYEL
DPEFSFANDQ PKNIATVLKD MKKGDIYKKL VDASDDEYAV NQSGQLSKKE GVYAIKLVDE
QETVRFDKQA YVSHILLSYK GAQKADEKVT RTQTDAFQAA KEVLAKIKAG EDFSTLAKTY
SDDPGSKNQG GVLPSPVNKS AQYVQVFKDA SLALKAEGDI SEITSSEFGY HIIKATKIET
DVKERQVKLE KVFFSTAADM WRTTGLDGSQ FTHADVNFDQ LYQPYVSIQF NAEGAKLFEE
ITGRNVEKPL AIFVGGEFIS SPTVKNKISG GSAQISGRFT VEDANNLARD LNTGAIPAPV
LLVGQHTIGS TIGQEALTKS VKAGLLGLLI VAIFMIVYYR LPGLLAVGAL SLYSLILIFL
IKSEINLIIA FLFSAIIFVA VTYKLLKANE PALEKILSFL LACFLLFFVA FLLRTPVTLT
LAGVAGVILS IGMAVDANIL IFERMKEELR SGKTLAAAVD AGFDRAWSSI RDSNYSSLLT
CAILFYLGSS IVKGFAFNLA AGIIVSMFTA ITITKTLLKA FIGTKYGQNL WLFGVKQGAK
ERPIIKFMSR SKIFLGASAT MITLGVIATL IFGFKPGLDF TGGTLMEFKF VNKDKVVTTE
TLKTALTEIG TELNKAVPIA TKTPAISPIA DKTTQSTELS STEEKLDLEN AQIISSGEDG
FIVKTKYISN ETHDKIVTEL KTKLDKNMEE LRFTTIGAVV GGSMQNKAIW AVVATCLMIM
LYLAFTFRKI PKHVNPWRFG IAAIIALVHD IWITIGVFVI IGYFTNFEID ILFITALLTI
LGFSVHDTIV VFDRLREHLR IDEKEDIETI ADISMTQTLS RSINTSLTAV LTLTAMLIFG
SSSIFYFILT LDIGIIIGTY SSIFIATPVV VYWTKWALNK KAAK
//
