SECF_RICCK
ID SECF_RICCK Reviewed; 310 AA.
AC A8EXI0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Protein translocase subunit SecF;
GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=A1E_00575;
OS Rickettsia canadensis (strain McKiel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=293613;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=McKiel;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia canadensis.";
RL Submitted (SEP-2007) 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: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-YajC and YidC. {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; CP000409; ABV73063.1; -; Genomic_DNA.
DR RefSeq; WP_012148264.1; NC_009879.1.
DR AlphaFoldDB; A8EXI0; -.
DR SMR; A8EXI0; -.
DR STRING; 293613.A1E_00575; -.
DR EnsemblBacteria; ABV73063; ABV73063; A1E_00575.
DR KEGG; rcm:A1E_00575; -.
DR eggNOG; COG0341; Bacteria.
DR HOGENOM; CLU_050012_1_1_5; -.
DR OMA; AFEWRMA; -.
DR OrthoDB; 410730at2; -.
DR Proteomes; UP000007056; 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; IPR022646; SecD/SecF_CS.
DR InterPro; IPR005665; SecF_bac.
DR PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF07549; Sec_GG; 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 Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..310
FT /note="Protein translocase subunit SecF"
FT /id="PRO_0000316281"
FT TRANSMEM 20..42
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
SQ SEQUENCE 310 AA; 35207 MW; 830EBD93981E61BA CRC64;
MQIYPLRLLP NKIDFDFMNF KKVSYTFSII LSLISVISIG IYKFNFGIDF VGGIVIEVRL
DQTPDLPKMR QILGELGIGE VVLQNFGSER DLSIRLGSSS EANLMENIEL IKASLHNNFP
YKFEYRKVDF VGPQVGRQLI EAGTMAMLFS FLAIMVYIWV RFEWYFGLGI LIALMHDLIL
ALGFMSMTKL DCNLSTIAAV LTIIGYSVND SVVIYDRIRE NLRKYYKKNI TEIINLSINE
TLSRTILTVI TTLLANLALI LFGGEAIRSF SVLVFFGIIA GTYSSIFISA PILTMFANKK
FNNKKFNNKR