(data stored in ACNUC5340 zone)

SWISSPROT: SECD_ACAM1

ID   SECD_ACAM1              Reviewed;         475 AA.
AC   B0CEA7;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 1.
DT   11-DEC-2019, entry version 67.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=AM1_0695;
OS   Acaryochloris marina (strain MBIC 11017).
OC   Bacteria; Cyanobacteria; Synechococcales; Acaryochloridaceae;
OC   Acaryochloris.
OX   NCBI_TaxID=329726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBIC 11017;
RX   PubMed=18252824; DOI=10.1073/pnas.0709772105;
RA   Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J.,
RA   Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D.,
RA   Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y.,
RA   Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M.,
RA   Blankenship R.E., Touchman J.W.;
RT   "Niche adaptation and genome expansion in the chlorophyll d-producing
RT   cyanobacterium Acaryochloris marina.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).
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   -!- FUNCTION: Probably participates in protein translocation into and
CC       across both the cytoplasmic and thylakoid membranes in cyanobacterial
CC       cells. {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}.
DR   EMBL; CP000828; ABW25741.1; -; Genomic_DNA.
DR   RefSeq; WP_012161329.1; NC_009925.1.
DR   SMR; B0CEA7; -.
DR   STRING; 329726.AM1_0695; -.
DR   PRIDE; B0CEA7; -.
DR   EnsemblBacteria; ABW25741; ABW25741; AM1_0695.
DR   KEGG; amr:AM1_0695; -.
DR   eggNOG; ENOG4107QN8; Bacteria.
DR   eggNOG; COG0342; LUCA.
DR   HOGENOM; HOG000018636; -.
DR   KO; K03072; -.
DR   OMA; APMEIIE; -.
DR   OrthoDB; 121331at2; -.
DR   Proteomes; UP000000268; 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:P-P-bond-hydrolysis-driven protein transmembrane transporter 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;
DR   PRODOM; B0CEA7.
DR   SWISS-2DPAGE; B0CEA7.
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..475
FT                   /note="Protein translocase subunit SecD"
FT                   /id="PRO_0000412669"
FT   TRANSMEM        7..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        305..327
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        334..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        357..377
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        402..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ   SEQUENCE   475 AA;  51067 MW;  2AAD14B0B9B6B9C2 CRC64;
     MLKQQRFLLA LIALLVVGAL IVVTPFGKQY GLGKINLGLD LRGGSQLTLQ VNPTEEVKDI
     TPNVMEAVQT VVANRLNPEG VSEIVVQTVG SQQILVQLPG VSDPKDAEQL LSQVAQLDFR
     RPNNAILAQV NVRSSELQRL LQKLPEAEKA GDAAALAKLQ GEVQQKQKQL TELQDQFFVK
     TDLTGEDLND AGYAISQSQP NKWDVTLRFD VDGGKKFAAL TKSLAGTGQP LGIFLDGKSI
     SQATVSDRFK ANGITGGAAI ITGNFELEDA KLLANQLKGG SLPVPVKVEE IRTVGATLGQ
     DSIRQSVYAG IGGLILVLIF MGVWYRLPGL IADVALCVYG LLTFACYVLF GVTLTLPGIA
     GFILSIGMAV DANILIFERT REELRSGKTL YRSIESGFYR AFTSILDSNV TTLIACGVLY
     WLGSGLVRGF AVTLGIGVAV SMFTAITCSR TLMFTAISLP NLRKIELFDS KRAVS
//

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