SECF_RICB8
ID SECF_RICB8 Reviewed; 303 AA.
AC A8GYD9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Protein translocase subunit SecF;
GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=A1I_01360;
OS Rickettsia bellii (strain OSU 85-389).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=391896;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OSU 85-389;
RA Madan A., Lee H., Madan A., Yoon J.-G., Ryu G.-Y., Dasch G., Ereemeva M.;
RT "Complete genome sequencing of Rickettsia bellii.";
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; CP000849; ABV78664.1; -; Genomic_DNA.
DR RefSeq; WP_011477843.1; NC_009883.1.
DR AlphaFoldDB; A8GYD9; -.
DR SMR; A8GYD9; -.
DR KEGG; rbo:A1I_01360; -.
DR HOGENOM; CLU_050012_1_1_5; -.
DR OMA; AFEWRMA; -.
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 InterPro; IPR000731; SSD.
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.
DR PROSITE; PS50156; SSD; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..303
FT /note="Protein translocase subunit SecF"
FT /id="PRO_0000316280"
FT TRANSMEM 28..48
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 303 AA; 34349 MW; 5016D954487DA3E6 CRC64;
MQIYPLRLLP NKIDFDFMNF KKVSYTFSII LSLISFIWIG MYKFNFGIDF AGGIVIEVRL
DQTPDLPKMR QVLGELGIGE VVLQNFGSER DLSIRFGSSS EDNLMKNIEL IKSTLQNNFP
YNFEYRKVDF VGPQVGRQLI EAGTMAMLFS FAAIMIYIWV RFEWYFGLGI LIALVHDVIL
ALGFMSITKL DFNLSTIAAV LTIIGYSVND SVVIYDRIRE NLRKYHKKGI TEIINLSINE
TLSRTILTVV TTLLANLALV LFGGEAIRSF SVLVFFGIIA GTYSSIFISA PILTIFANKK
FEK
