ID A0A176T6X7_9FLAO Unreviewed; 991 AA.
AC A0A176T6X7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=LPB303_13600 {ECO:0000313|EMBL:OAD43115.1};
OS Polaribacter atrinae.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1333662 {ECO:0000313|EMBL:OAD43115.1, ECO:0000313|Proteomes:UP000076923};
RN [1] {ECO:0000313|EMBL:OAD43115.1, ECO:0000313|Proteomes:UP000076923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 17473 {ECO:0000313|EMBL:OAD43115.1,
RC ECO:0000313|Proteomes:UP000076923};
RA Shin S.-K., Yi H.;
RT "Draft genome sequence of Polaribacter atrinae KACC17473.";
RL Submitted (FEB-2016) 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: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:OAD43115.1}.
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DR EMBL; LVWE01000056; OAD43115.1; -; Genomic_DNA.
DR RefSeq; WP_068451242.1; NZ_LVWE01000056.1.
DR AlphaFoldDB; A0A176T6X7; -.
DR STRING; 1333662.LPB303_13600; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000076923; Unassembled WGS sequence.
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; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
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; 1.
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:UP000076923};
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 504..522
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 553..574
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 595..622
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 628..652
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 686..707
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 822..840
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 847..873
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 879..896
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 933..951
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 957..981
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 192..248
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 482..652
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 805..984
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 991 AA; 108323 MW; D3450F0E433C050D CRC64;
MQNKGLIKLF AILFGLVSLY QLSFTFLATK VEDDAAAYAE SKGDNIDARQ KATFERKYLD
SVANKDIINL GVTTYTYNDV KDKEMNLGLD LKGGINAILQ VSVKEVLKSL ANDSKNVAFN
QALEAADEAQ KNSNATYLDL FFQEFEKVAG DTKLSDPSIF GTKALSEKIT FNEANATVKQ
TLQEEINSSI GTAFEVLRSR IDKFGVTQPN IQRIGNSGRI QIELPGAKDI ERVTRLITSK
AELQFWEVYT NAEVQNYFFT ANGKIAEILK DDTAAEKVID STKKDDIDDL LGESIDSTDV
SQKNLFTYFF PNIAQSQQQM SSLVGQARVL DTAMVNSLLN RKDVKALLPN ELKYVKFLWD
YKSNKGTDGT ELIGLYAIKG NRSGNATIEG DVILDASQVF DQLNKPEVSM TMNSSGTKQW
AKMTTENQGK FVAVVLDNYV YTAPSVNTPI TGGRTSISGG SMTITEAEDI ATVLKAGKLP
AAARIIQAEV VGPSLGQESI DHSIQSFGLA ILLVLVWMIL YYGKAGLYAD IALAVNILFI
FGILASFNAV LTLPGIAGII LTIGMSVDAN VIIFERIKES LAIKKGLKQS VEEGFSIKGA
LSAIIDANIT TLLTGVILYV FGTGPIKGFA LTLMIGIATS LFTAVFITRL LIDKSVNKGA
NLTFNTSISK GWFQNINVEF LRKRKIAYII SGAVIIAGIV SIFSVGLKQG VDFKGGRSYV
VRFDQTMNAT EVASTLKDAF GTAPEVKTYG SDHQLKITTV YKIDEDGQDV DDQVQSALFT
GLKSYLGTTT YEDFKPGFEK EGSGVMSYMK VEPTIADDIK TSALYAVFGS LLVVFLYILL
RFRKISFSIG AVIAVFHDVL IVLSVFSITY SFMPFDMEIG QSFIAAILTV VGYSLNDTVV
IFDRIREFTG THPNWKYSEV VDKALSSTLG RTINTSLTTL LVMLAIFLFG GDSIKGFMFA
LIIGVVVGTY SSLFVATPIM FDTTKKEEKN N
//
