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Database: UniProt
Entry: A0A090Q3E7_9FLAO
LinkDB: A0A090Q3E7_9FLAO
Original site: A0A090Q3E7_9FLAO 
ID   A0A090Q3E7_9FLAO        Unreviewed;      1012 AA.
AC   A0A090Q3E7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, 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=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   ORFNames=JCM19294_1781 {ECO:0000313|EMBL:GAK96268.1};
OS   Nonlabens tegetincola.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=323273 {ECO:0000313|EMBL:GAK96268.1, ECO:0000313|Proteomes:UP000029221};
RN   [1] {ECO:0000313|EMBL:GAK96268.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19294 {ECO:0000313|EMBL:GAK96268.1};
RA   Nakanishi M., Meirelles P., Suzuki R., Takatani N., Mino S., Suda W.,
RA   Oshima K., Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L.,
RA   Niwa A., Sawabe T., Sawabe T.;
RT   "Draft Genome Sequences of Marine Flavobacterium Nonlabens Strains NR17,
RT   NR24, NR27, NR32, NR33, and Ara13.";
RL   Genome Announc. 2:e01165-14(2014).
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:GAK96268.1}.
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DR   EMBL; BBML01000002; GAK96268.1; -; Genomic_DNA.
DR   RefSeq; WP_042277473.1; NZ_BBML01000002.1.
DR   AlphaFoldDB; A0A090Q3E7; -.
DR   STRING; 319236.BST91_08825; -.
DR   eggNOG; COG0341; Bacteria.
DR   eggNOG; COG0342; Bacteria.
DR   Proteomes; UP000029221; 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; 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; 1.
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:UP000029221};
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        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        515..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        539..559
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        565..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        607..631
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        643..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        696..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        835..853
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        860..883
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        895..915
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        946..964
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        970..994
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          192..249
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          493..660
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   DOMAIN          817..997
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   1012 AA;  110175 MW;  C3E2B2B6C5DEF9CE CRC64;
     MQNKGLIRFF AIIFAVVSIY QLTYTFITNK VEDDAEAYAA TVVPADAENK SQLKSEAVKS
     YLDSVAKKDV WGGYTDYESA KKQELKKGLD LKGGINVILQ ISVKDILIGM ADESNDPAFR
     KALAAADERI KDGQDDYINY FLEEFNKIEG AQLASPDIFG TPEMEDAFEI DFQSSNADVA
     AVLKEELKDY LTSALDVIRK RIDQFGTTQP NIQQLGTSGR VLIELPGETD VKRIKDILTK
     AAQLEFWHVY KQGEISDYIV ASNNYWKEKL ATTSNVVEAD AVAADSTVVE EEDPADLSAL
     LDGDDETSEE VAETNLDENP ILGRLVRPSF IGGLGVFRAS DIDLILDYLN DPQSRARLSP
     ETRNAKFAFT LPTLDENLGF EVSDLFALVG NAEDEAPLAG GVITDAKQDY DLGAKVIVSM
     TMNGEGSKVW EEMTGYAFNN RSQVAVVLDN TVYSAPSVTT GPISGGSTQI SGSFTVQEAK
     DLATVLRAGK LPAKAEIIQS DVIGPSLGQE AIDSGLMSFA LALILVLIWM FFYYGRAGLY
     ADIALVVNIL FIFGALASLK AVLTLPGIAG IVLTIGISVD ANVLIFERIR EELAKGKSQA
     DSIKDGFNNA LSSILDANIT TLLTAIILYI FGTGPIQGFA TTLMIGILTS LFTAVFITRL
     FVDGYVKNGK TLTFASGVTK NWFRNVNIDF LKKRKVAYLV SLVVVIGSIA SLAINKLNLG
     IDFSGGRTYV VRFDQEVNAT EITKILSSED FLGSAEAKTY GDANQLKIST KYGIDQDDSV
     ISEEIESKLY VALKDFLPAD MTQTQFADVG SEVKTSGIMS NFQVGPTIAD DILKGSIYAI
     LGSLAVVFLY ILIRFKRWQF SLGAVVAVFH DVAIVLGVFS ALYKVLPFNM EIDQAFIAAI
     LTVIGYSLND TVVVFDRIRE FINERTGMAF GETVNRAISS TISRTLNTSL TTLIVLLAIF
     TFGGESIRGF MFALIVGVVV GTYSSVFIAT PVMYDTIKKS NGKIEADKKL EE
//
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