ID A0A1G2BR02_9BACT Unreviewed; 558 AA.
AC A0A1G2BR02;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=A3H70_05390 {ECO:0000313|EMBL:OGY91531.1};
OS Candidatus Komeilibacteria bacterium RIFCSPLOWO2_02_FULL_48_11.
OC Bacteria; Candidatus Komeilibacteria.
OX NCBI_TaxID=1798553 {ECO:0000313|EMBL:OGY91531.1, ECO:0000313|Proteomes:UP000178109};
RN [1] {ECO:0000313|EMBL:OGY91531.1, ECO:0000313|Proteomes:UP000178109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGY91531.1}.
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DR EMBL; MHKO01000044; OGY91531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2BR02; -.
DR STRING; 1798553.A3H70_05390; -.
DR Proteomes; UP000178109; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
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; 3.10.50.40; -; 1.
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 InterPro; IPR001036; Acrflvin-R.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR000297; PPIase_PpiC.
DR InterPro; IPR023058; PPIase_PpiC_CS.
DR InterPro; IPR005791; SecD.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR048631; SecD_1st.
DR InterPro; IPR048634; SecD_SecF_C.
DR NCBIfam; TIGR00916; 2A0604s01; 1.
DR NCBIfam; TIGR01129; secD; 1.
DR PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF13616; Rotamase_3; 1.
DR Pfam; PF21760; SecD_1st; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01463}; Isomerase {ECO:0000256|PROSITE-ProRule:PRU00278};
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}; Rotamase {ECO:0000256|PROSITE-ProRule:PRU00278};
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 394..412
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 443..464
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 495..511
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 517..540
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 135..241
FT /note="PpiC"
FT /evidence="ECO:0000259|PROSITE:PS50198"
SQ SEQUENCE 558 AA; 61321 MW; 702634A6D61650DF CRC64;
MTSPRQQIWI LFFLLAGLGF ISGSIFTPTL PAWWPGYTWF GRFRAHLGWD LQGGAHLIYQ
ADTSKVSFDE AKSAIAGVRD VIEKRVNALG VSEPVIQTAT VGNKLRVIVE LAGVFDVNEA
IKQIGATPLL EFKTETPEPA KQELTAEEKK KREEFNKAQL KKTEDAIKQL AASEGQNFAE
LATKVSEDTG SASQGGDLGF IKKESLVEPF AAVLFDQLKD GEMTLEPVAT QFGYHIIQRL
ESKTENNEIL VRSRHILFLT QSLEGDTPQV DPWANTQLGG RQLKKSEVQF DQMSGSPSVG
LIFNDDGAKL FEDLTRNNVG KRVAIFLDNN LLSAPVVQSE ISGGKAVITG NFSIPEARQL
VQRLNAGALP VPINLVSQQT VGPSLGQVSI DKSLQAGIIG FILVAIFMLA FYRFAGFLAV
IALTFYASIV FALFKLIPVT LTLAGIAGFV LSVGMAVDAN ILIFERLREE LRRGEPFERA
LKEGFLRAWH SIRDSNVSSL ITCMILAWLG TSVVKGFAIT LAIGILASMF SAITITRFLM
EIFSRAAWLR DKKWFWGA
//
