ID A0A0F9ZK32_9BACT Unreviewed; 1047 AA.
AC A0A0F9ZK32;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=UR28_C0009G0020 {ECO:0000313|EMBL:KKP39196.1};
OS Candidatus Peregrinibacteria bacterium GW2011_GWF2_33_10.
OC Bacteria; Candidatus Peregrinibacteria.
OX NCBI_TaxID=1619065 {ECO:0000313|EMBL:KKP39196.1, ECO:0000313|Proteomes:UP000034183};
RN [1] {ECO:0000313|EMBL:KKP39196.1, ECO:0000313|Proteomes:UP000034183}
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:KKP39196.1}.
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DR EMBL; LBOP01000009; KKP39196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F9ZK32; -.
DR PATRIC; fig|1619065.3.peg.496; -.
DR Proteomes; UP000034183; 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 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.
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 5..22
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 510..528
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 533..550
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 556..575
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 582..602
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 608..630
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 664..682
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 688..707
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 744..765
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 874..893
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 905..927
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 939..959
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 991..1008
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 1014..1039
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 251..362
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 1047 AA; 115969 MW; 5F74295360D1BE72 CRC64;
MKRNILIKIL IIVIFAIGLG FLDLPSEYQQ KVIPNLPQSL KEMKYNLGLD LQGGTQLTYK
IDLNKVDPSQ RQKIIEGVKE VITKRVNGLG VNEPYIYVSD FGGEKYIVVE LAGIKDIEKA
KATVGKVIQL EFKTQKNTSD ASEIEVVRVA ANDTLKKIKN GTAISQIGPE LQSANPQKVQ
YIENKDYVYQ DQLVPTIQNV LAKLPVGKIF SEIVEGNNGK FLDSSGLKDQ TGFFVLQLVD
KKTQDREIKH DKSIKVSHLL ISYKGAERAA LTVTRSKEEA QKLAKEVLTK LQAGEDFSTL
VNEYSDDLSN KDKGGILDQE VNKDSQYDPD FIAGALDLQN NNEISQKPVE TKFGFHLIKA
DKVTPEYTET KSEEAYKLQE IFFSTLPDPW QDTELNGEYF ESASVAFNNL YVPYVSIKFN
DEGAKIFEKL TEENINKPLA IFVGGELISA PNVQQKISGG QAQITGNFSV DEANKLARDL
MTGAIPAPIT LSGQYTLGAS IGEQALNASF KAGLIGIIVL ALFMILYYRL PGLIANIALT
IYAIILAFLI KMSIPMIAST LIAAVIYVFI IIKIVQSEEN GLEKLASFVI ATFAFFFLAF
LFSTSITLTL AGFAGIVLSV GMAVDANILI FERMKEEMRN GSTYSMAIVA GFNRAWPSIR
DSNFTTLIIC AILIVFGSSI IRGFAFNLAA GVVVSMFTAI SISYVFLQGL KYTPLKEYPW
LFGGPRAGKE YKKPDLKIMK YRKFFYGLSV ASILPGLIGL AIWGFNYGMD FKGGTLLEIK
FPNTVTNIQI QEELKKFDDE YNKDLSDETK KIDLSVNPQI IASGENTFII RHKSIEEEVH
QKLLTKLKTD FGTIEELRFT TIGPTVGATL KKKALTSLTI ALIAIMSYIA FAFRKVPKQI
SAWKFGIAAI IALAHDLACL VGIYVIIGHF LPAAEIDTLF ITALLTLAGF SVHDTIVVFD
RLRENLKIHK TSTDLLALTD TSINETLHRS INTSLSTVIP LIAMYFLGSD SIQFFVLSLI
IGITVGAYSS IFIASPLLIE FERFKRK
//
