ID A0A1I2E1G6_9BACT Unreviewed; 1056 AA.
AC A0A1I2E1G6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN05518672_11192 {ECO:0000313|EMBL:SFE86496.1};
OS Chitinophaga sp. CF118.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1884367 {ECO:0000313|EMBL:SFE86496.1, ECO:0000313|Proteomes:UP000199596};
RN [1] {ECO:0000313|EMBL:SFE86496.1, ECO:0000313|Proteomes:UP000199596}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF118 {ECO:0000313|EMBL:SFE86496.1,
RC ECO:0000313|Proteomes:UP000199596};
RA de Groot N.N.;
RL Submitted (OCT-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}.
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DR EMBL; FOMK01000011; SFE86496.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2E1G6; -.
DR STRING; 1884367.SAMN05518672_11192; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000199596; 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; 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};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 579..601
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 607..629
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 650..671
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 677..701
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 736..756
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 867..885
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 892..913
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 928..947
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 980..998
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 1004..1028
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 209..265
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 535..701
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 847..1032
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 1056 AA; 116466 MW; 3901C49DE1A88995 CRC64;
MQLKGLVRFF AGALILISVY YLSFTFLVRN YEKKIDAQAL SDISKAYPSA EQKYPGNKEL
QAFYQDSLTE MIKLRRQRLL DSTSNKEMAG FPWYVNYTKA KERELNLGLD LQGGMNVVLD
VSVEDVIRSL SGQSKDPAFN KALDLATQRK KSSQSDFVTL FGQAYEEVAA NGRLATIFAN
AYQKDINFNS SNQQVLDVIR REAGAAIKNT YLVLQKRIDK FGVASPNISL DENKGIISVE
LAGVDNPERV RRYLQATANL EFREVYKNGQ EFVTNVLQPM NEAVKNSLSG KKAVDSVKTT
DSTTVAAKAA EDTSKEGSLA SYLSKDSGKG KGVDSAKTKA DMEREAIAAN PLFAIFHPSI
TQDGRIVPSP VVGSIYPTDT ATFKRYLLLP AVRNILPKDI VFAYGPENKE DRHGPLEVYA
LKINPANPTP RVGGESVVDA RQDFDQNGNP EISMTMDAVG AREWKKLTGE LAPSNPDDRA
TFSYVAVVLD SIVYSAPSIL NEIAGGRSSI TGSFTLEEAK DLANILKSGK MPAPAKIVQE
MVVGPTLGAE SIAAGAKSFM ISFVVIFVLM LVYYNSAGWV ANIALILNLL FTFGILASLG
ATLTMPGIAG LVLTIGMAVD TNVIIFERIK DELARGKTYQ QAVEDGYKKS YAPILDGHVT
SLLTACILFY FGLGPVLGFA TTQIIGLLLS LFCGIMVSRI VTDFWTNKKR HFQYFTPISQ
KIFKHASFDF VGKRKYAYVI STVMILLGAS SFFHGFRHGV DFDGGRNYTV RFDQPVKTEE
VRADLEKAFG SEPFVKTIGN TNQLNITTNY KIDEQSLAVD KEVTEKLYQG LKKFYDPSVT
YEIFSSNRYI VASQTVSPTI SDDLRAGAVK ATILSLVVIF LYILLRFSKW QYSIGTIFSL
LHDVMVTLAV FSYCRDFVPF SLEIDQHFIA AILTVIGFSM NDTVIVFDRI REYFRNGTFK
GESRDFVINK AINATLSRTV MTSLTVFLTI LILFIFGGEV TRGFAFAMLI GVVTGTYSSI
FVAAPVLVDF DKKNQLSNES DAIAAKVVSE PAPAKK
//
