SECD_AQUAE
ID SECD_AQUAE Reviewed; 501 AA.
AC O67102;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=aq_973;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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}.
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DR EMBL; AE000657; AAC07060.1; -; Genomic_DNA.
DR PIR; C70384; C70384.
DR RefSeq; NP_213665.1; NC_000918.1.
DR RefSeq; WP_010880603.1; NC_000918.1.
DR AlphaFoldDB; O67102; -.
DR SMR; O67102; -.
DR STRING; 224324.aq_973; -.
DR EnsemblBacteria; AAC07060; AAC07060; aq_973.
DR KEGG; aae:aq_973; -.
DR PATRIC; fig|224324.8.peg.765; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_0; -.
DR InParanoid; O67102; -.
DR OMA; MVVYYRL; -.
DR OrthoDB; 121331at2; -.
DR Proteomes; UP000000798; 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:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01463_B; SecD_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 PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
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..501
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000095956"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 447..467
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 470..490
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ SEQUENCE 501 AA; 55459 MW; E129FC97445D6C97 CRC64;
MILIMQKKNL WLHLLGLVIL TLLSAYAVVK YPINLGLDLK GGVEFLLEPD FSVAIEREYE
DLARNLREKL SKFNVLEVYA TKEGVIIELL DKKEVENIKK VIQDINPNVI FEEEGDKLVV
KFTQKYVEQL KEDIVRQSIE IIRDRIDKLG VTQPVVTRVG KYRILVDLPG FLDVERAKKI
IGSTASLELK LVIDVSTDRK ELEKKLTPDR EILPSRDGRE WFLVEKAPVI TGQDLKTAYV
GVDNLGQPAV NFELKGEAAE KFGKFTEQNI GKRLAIVLDR KVVSAPVIRS KISDRGQITG
NFTAQEARDL ALILRTGSLP SPLKFLQEKI VGPSLGKDAI EQGIKAGILA IILLAVVLIA
RYKTAGITAN ISIFLNVLFL LASMAFLGAT LTLPGIAGII LNMGIAVDSN VLIFERVKEE
LRLGNTVSKA IELGFKRTLS AVWDTHVTLL VASVILFQFG SGPVKGFATT LALGTIASFI
SNVYYAKVFL DLLNSLKILK I