ID A0A1W2AF44_9SPHI Unreviewed; 993 AA.
AC A0A1W2AF44;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
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=SAMN04488101_101517 {ECO:0000313|EMBL:SMC58878.1};
OS Pedobacter nyackensis.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=475255 {ECO:0000313|EMBL:SMC58878.1, ECO:0000313|Proteomes:UP000192678};
RN [1] {ECO:0000313|EMBL:SMC58878.1, ECO:0000313|Proteomes:UP000192678}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19625 {ECO:0000313|EMBL:SMC58878.1,
RC ECO:0000313|Proteomes:UP000192678};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) 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; FWYB01000001; SMC58878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2AF44; -.
DR STRING; 475255.SAMN04488101_101517; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000192678; 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; 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:UP000192678};
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 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 513..532
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 539..560
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 566..587
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 636..660
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 694..711
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 815..836
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 843..864
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 879..898
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 934..953
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 959..982
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 178..235
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 498..659
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 791..986
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 993 AA; 107916 MW; 000CC1BFD5577902 CRC64;
MQGKGFIKFM AILLGIVCVY SLSFNFVTSK VEKDAKAYAK GDVEKEKAYL DSMATVPVYP
LFGFNYQFCK GKEINLGLDL KGGMNVTMEI SLGELVKSLA GNTDDVNFNK ALAAAQQRLN
AGGKDYVSLF VDEYEKLAPN SQLVDFFSNQ DNAKLLKPNA SNAEVKTFLS KEATSAIDRS
FIIIRSRIDG FGVVSPNMQK QEGTNRILIE MPGVQDKERV HKLLQGSAEL QFWQVYQNEE
VYPVLENINK TLATTLKHTT KDTSSAAGAK DTTAKAGSKL AGLAKTTDTK DSANVKNNEL
AKSNPLFAIL NIPTYQGENG QPALRPGPVV GWVAQKDTAK VNAFLKRPEI AAIIPQTYKF
MWSVKPADLG TQTPSKIFEL YAIKVTSLDG KPDLGGEAIS DARSDFDQHG KPEVTMYMTG
DGASKWKKIT AEASADANNK KAIAIVLDNT VYSAPTVQNE IAGGVSQITG NFTQNDTQDL
ANILKAGKLP APARIVGEFV VGPSLGEVAI HNGLLSFVLA FVVILIFMAV YYNKAGWVAN
LALVINLFFI MGILVSLGAV LTLPGIAGIV LVIGLSVDAN ILIFERVREE LTLGKSTPVA
IKEGFKHAMS SIIDSNVTVL VLGVILYVFG SGPVQGFATT LCIGILSSLF CAVLISRIVF
ETLLDKKVDI TFGNKYTIHA FKNIAFNFVG HRKLYYTISA VIIALGVIFY IKNDGLNLGI
DFKGGRTYIV HFDKGMHTED VKAKLNSVFP ESETIVKTAG GDNELKITTT YHITDTDTEA
DKIVETALKS GLDQTGAKYT IESNEKVGPI IASDILYSAY GAILFSCLVM FIYIVVRFKK
LNYGLGAVIA LFHDVLLVLS FYTILDGVLP FSLEIGQDFI AAILTVMGYT MTETVVVFDR
IREKLTEAGK DDLHGKEKEN LINFALNSTL SRTILTSLTV FFVLLVIFVF GGASIRGFIF
ALLIGRIIGT YSSLCISTPI VLDLGEANVK VKK
//
