ID   SECD_KORVE              Reviewed;         535 AA.
AC   Q1IVE9;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000255|HAMAP-Rule:MF_01463};
GN   OrderedLocusNames=Acid345_0146;
OS   Koribacter versatilis (strain Ellin345).
OC   Bacteria; Acidobacteria; Acidobacteriales; Acidobacteriaceae;
OC   Candidatus Koribacter.
OX   NCBI_TaxID=204669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ellin345;
RX   PubMed=19201974; DOI=10.1128/aem.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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_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:0000255|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01463}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000360; ABF39151.1; -; Genomic_DNA.
DR   RefSeq; WP_011520953.1; NC_008009.1.
DR   AlphaFoldDB; Q1IVE9; -.
DR   SMR; Q1IVE9; -.
DR   STRING; 204669.Acid345_0146; -.
DR   EnsemblBacteria; ABF39151; ABF39151; Acid345_0146.
DR   KEGG; aba:Acid345_0146; -.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_4_3_0; -.
DR   OMA; MVVYYRL; -.
DR   OrthoDB; 121331at2; -.
DR   Proteomes; UP000002432; 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_01463_B; SecD_B; 1.
DR   InterPro; IPR001036; Acrflvin-R.
DR   InterPro; IPR005791; SecD.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   PANTHER; PTHR30081; PTHR30081; 1.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 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..535
FT                   /note="Protein translocase subunit SecD"
FT                   /id="PRO_5000120802"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        402..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        425..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ   SEQUENCE   535 AA;  57851 MW;  4578E85C400617AA CRC64;
     MKKNLTWKVV VIVAVLLVFA FGIIGNPAEV KWDKEGLKTA LMNRIHLGLD LRGGTHLILQ
     VVVNDAVNAE TDRAIERIKE DLANNKVTYS DITKPDAANA PERIAIKGIT PDGATTLRRV
     SDERLPEYSF GSGPEGSYTL TMKPAQLKDL KDRAVQQAIQ KIRERVDSLG VSEPVIQEHG
     LGDYQILVQL PGVDDPARVK EVMQSTAMLE IRQVFGGPYS KESEAAQGQM QQPDTVVLPG
     KSESDPGTQV FYLVARSSAV AGHDLRQARV GRDQNGGANV QFNLTRDGGV RFSQFTSAHV
     GDKLGVILDG KVMEVANIKS EISDSGEIEG RFTDQQASDL ALILNSGALP ASIKYLEERT
     VGPSLGMDSI RQGVRAAIIG FVAVIIFMLI YYKGAGINAD LSLLLNLVIL LGFMGYFGAV
     LTLPGIAGVI LTVGMGVDSN VLIFERIREE LRNGKTPPSA VEQGFGHAWL TIIDTHVTTI
     VSAIILFLFG TGPVKGFAVT LSFGLFANLF TAVFVSRVIF DSILNRHQRG EALSI