ID A0A3E1NJZ9_9BACT Unreviewed; 1042 AA.
AC A0A3E1NJZ9;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=DXN05_11550 {ECO:0000313|EMBL:RFM28154.1};
OS Deminuibacter soli.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Deminuibacter.
OX NCBI_TaxID=2291815 {ECO:0000313|EMBL:RFM28154.1, ECO:0000313|Proteomes:UP000261284};
RN [1] {ECO:0000313|EMBL:RFM28154.1, ECO:0000313|Proteomes:UP000261284}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K23C18032701 {ECO:0000313|EMBL:RFM28154.1,
RC ECO:0000313|Proteomes:UP000261284};
RA Wang C.;
RT "Chitinophagaceae sp. K23C18032701, a novel bacterium isolated from forest
RT soil.";
RL Submitted (AUG-2018) 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:RFM28154.1}.
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DR EMBL; QTJU01000003; RFM28154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E1NJZ9; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000261284; 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}; Reference proteome {ECO:0000313|Proteomes:UP000261284};
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 538..563
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 570..592
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 598..620
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 641..662
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 668..692
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 857..875
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 882..904
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 916..937
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 968..986
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 992..1016
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 207..263
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 526..692
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 837..1020
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 1042 AA; 113802 MW; 7D266CECB7E33344 CRC64;
MQLKGLVRFF TIALILICLY QLSFTWIVRS HESSMGEKAD KYMSANYQKP EQKYSDKDMQ
AAYADSLKQI RDEKFHRLLD STKDTKIGPF GLTTYQSAQD NELKLGLDLQ GGMSVTMEVG
LDGLIRSLAD NTKDPNFNKA LAQAVARKAN GGADLITLFN EELQKVSPGT KLAPFFASRS
NNVIKYDASD AKVLDYLKTQ ATTAFNNTYR ILRTRIDRFG VASPTINPDP AKGIITIELA
GVNDAERVRR YLQSTANLQF FEVYNIGEVG ESVLAADKAL SEYLKGNKAV AATDTTAAAS
GYAANTDTAA KAADTTKVSS LSQLGNAKTG TAAAVKDSNQ IRQEEAPLRS MVYFEQGQRT
QAGGVQFPSN IGRVLVKDTA QIGAYLRMDI VRNKFPSNLA FMYGKADSED PKAKNVLSLY
AIKTLDNGSA PLEGEHVSES RQDYDERGRV AIKMSMDPIG TRIWAKLTEK NVGKPIAIVL
DNIVYSAPFV NGPIPNGSSE ISGSYSLVEA QDLADILQSG KLPAPAKIVQ EQIVGATLGI
AAVKGGGLAF AISFVVIFAL MLVYYNTAGW VANIALILNL LFTIGVLSAL GFTLTAPGIA
GLVLTIGMAV DTNVIIFERI KEELTKGSDY KTAVANGYKR SYAPVLDAHV TTLLTAIILA
YFGLGPVLGF ATTQIIGILL SLFCGILVSR LISDIYTNKN RHFNYFTGIS KRVFKHASYK
FIEYRKVTYI ISGIVLLLGI ASFFNGFDEG VEFEGGRSYT VQFDKAPSHD AVLNDLKEVF
GEYPTVKTVD KPTQLNITTA YRIHETGNNV DSAVEATLYK GLTKFLPQGL SFKDFQAKYK
QRSQTVLPTI SDELKSGATK ATVISILVIC LYIFIRFRDW RYSLGTIVSL LHDVFVTLAV
FSFLRKVVPF PLEIDQHFIA AILTVIGFSM NDTVIVYDRI REDSRIMKGE SKGTIINRAI
NQTLSRTVMT SLTVFLTILI LFLVGGEVTK GFAFAMLIGV VTGTYSSIFV AAPILVDFAK
DKPLGKPEEE AKKPQAAATV KG
//
