ID SECDF_BRUAB Reviewed; 758 AA.
AC P0C117; Q57DL6; Q9ZG86;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Protein translocase subunit SecDF;
GN Name=secDF; OrderedLocusNames=BruAb1_0903;
OS Brucella abortus biovar 1 (strain 9-941).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=262698;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9-941;
RX PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT "Completion of the genome sequence of Brucella abortus and comparison to
RT the highly similar genomes of Brucella melitensis and Brucella suis.";
RL J. Bacteriol. 187:2715-2726(2005).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the essential Sec protein translocation apparatus
CC which comprises SecA, SecYEG and auxiliary proteins SecDF-YajC and
CC YidC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SecD/SecF family.
CC SecD subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the SecD/SecF family.
CC SecF subfamily. {ECO:0000305}.
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DR EMBL; AE017223; AAX74268.1; -; Genomic_DNA.
DR RefSeq; WP_002969411.1; NC_006932.1.
DR AlphaFoldDB; P0C117; -.
DR SMR; P0C117; -.
DR EnsemblBacteria; AAX74268; AAX74268; BruAb1_0903.
DR GeneID; 3787582; -.
DR KEGG; bmb:BruAb1_0903; -.
DR HOGENOM; CLU_007894_2_1_5; -.
DR Proteomes; UP000000540; Chromosome I.
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; 3.30.70.3400; -; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
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 inner membrane; Cell membrane; Membrane; Protein transport;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..758
FT /note="Protein translocase subunit SecDF"
FT /id="PRO_0000095958"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..426
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..599
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 706..726
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 758 AA; 81982 MW; 297DF4D28259901F CRC64;
MLYFSRWKSA LIWLAVLVSL IIASPNFFSR ETLENLPDFL PKKQVSLGLD LSGGSRLILQ
VQNAGKTDLE TTANIMRQRL EELGYGNPVV EGEGRNQIRV EVPGLYDAQL LKDILTIRGN
LSFRAMDDTM SPDDAIRGTP PADSEIVYSF DDPPVGYLLK KTPILTGHDI TDAKASISAD
DGQPVITLTL DDNGRRRLAD LTAQGNENSF AIVVDNQVVS APTVSGPLDT SELQIEGAFD
LQAANNMAVV LRSGALPQAV TVLEERTIAS ALGEDYASAA VLAALLAALV VGLFMVLSYG
ILGVIALVAL VVNIVILTAV LSLIGASISL ASIAGLVLTI GLAVDAHILI YERVREDRRK
GYSVVQAMES GFYRALSTIV DANLTTLIAA LVLFLLGSGT VHGFALTVAI GIGTTLFTTL
TFTRLLIAQW VRTAKPKEVP KRRLKLVPTV THIPFMRLQF VTLGISVLAC AIVVALFVNI
GFNYGIDFRG GSMVELQARN GDANLEDINE RLAELNIDSA RVLPAKSPRS ALVIIGSQEV
GDDAEQTVAV KLRGEFEQDY SFQRVDVVGP TVSEQLSRAG VLAVILSLIG IFIYVWFRFR
WQLALGAVLS TLHDVVILSG MFIVFRMEFN LWSVAAILTI IGYSLNDTVV IYDRVRENLR
RYKSAPLPAI IDASINQTLS RTLLTSFVTF LAHVPLYAFG GSEIRMFALA LSVGIIVASY
SSIFIAAPLL VQFGLKPRET DAGDAVDAEL AQSLNLES
//
