SECF_BORBU
ID SECF_BORBU Reviewed; 299 AA.
AC O51597;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Protein translocase subunit SecF;
GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=BB_0653;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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:0000255|HAMAP-Rule:MF_01464}.
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:0000255|HAMAP-Rule:MF_01464}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01464}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01464}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01464}.
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DR EMBL; AE000783; AAC66992.1; -; Genomic_DNA.
DR PIR; D70181; D70181.
DR RefSeq; NP_212787.1; NC_001318.1.
DR RefSeq; WP_002665673.1; NC_001318.1.
DR AlphaFoldDB; O51597; -.
DR SMR; O51597; -.
DR STRING; 224326.BB_0653; -.
DR PRIDE; O51597; -.
DR EnsemblBacteria; AAC66992; AAC66992; BB_0653.
DR KEGG; bbu:BB_0653; -.
DR PATRIC; fig|224326.49.peg.1044; -.
DR HOGENOM; CLU_050012_0_1_12; -.
DR OMA; AFEWRMA; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 HAMAP; MF_01464_B; SecF_B; 1.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR005665; SecF_bac.
DR PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR01755; SECFTRNLCASE.
DR TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR00966; 3a0501s07; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..299
FT /note="Protein translocase subunit SecF"
FT /id="PRO_0000095975"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
SQ SEQUENCE 299 AA; 34057 MW; DD9F9E51B1ABA68B CRC64;
MQRVINFSKY GSNVLIVSAV LILVGLIYTF FYHGGYNWGI DFSSRVNINL SIEKSNIKEN
EIKKIFSPIY KTLDVNSIFS PDQNKSEFSI MVKSDVIDYA FKTEVQKTIL DKLKETFDAN
IEVLDSYFID SSFSSTLRIR SIFLVLGTFI LILIYITLRF KLSYAIASIL SIFHDIFFIV
AFLGVFRIEI NSYIIVAILT IIGYSLNDTI IIFDRIRDNV KRLTDNTFLN VLNISISQTL
SRTVLTSVTT FVAVFSIYVF TEGSIKDFSL VFMVGVIVGT YSSVFIASPI LLNLYKKIK