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Database: UniProt
Entry: K9SFP1_9CYAN
LinkDB: K9SFP1_9CYAN
Original site: K9SFP1_9CYAN 
ID   K9SFP1_9CYAN            Unreviewed;       484 AA.
AC   K9SFP1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-SEP-2017, entry version 27.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=Pse7367_0295 {ECO:0000313|EMBL:AFY68609.1};
OS   Pseudanabaena sp. PCC 7367.
OC   Bacteria; Cyanobacteria; Synechococcales; Pseudanabaenaceae;
OC   Pseudanabaena.
OX   NCBI_TaxID=82654 {ECO:0000313|EMBL:AFY68609.1, ECO:0000313|Proteomes:UP000010386};
RN   [1] {ECO:0000313|EMBL:AFY68609.1, ECO:0000313|Proteomes:UP000010386}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7367 {ECO:0000313|EMBL:AFY68609.1,
RC   ECO:0000313|Proteomes:UP000010386};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y.,
RA   Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A.,
RA   Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Pseudanabaena sp. PCC 7367.";
RL   Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. SecDF uses the
CC       proton motive force (PMF) to complete protein translocation after
CC       the ATP-dependent function of SecA. {ECO:0000256|HAMAP-
CC       Rule:MF_01463, ECO:0000256|SAAS:SAAS00541769}.
CC   -!- FUNCTION: Probably participates in protein translocation into and
CC       across both the cytoplasmic and thylakoid membranes in
CC       cyanobacterial cells. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec
CC       protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP003592; AFY68609.1; -; Genomic_DNA.
DR   RefSeq; WP_015163583.1; NC_019701.1.
DR   EnsemblBacteria; AFY68609; AFY68609; Pse7367_0295.
DR   KEGG; pseu:Pse7367_0295; -.
DR   PATRIC; fig|82654.3.peg.335; -.
DR   KO; K03072; -.
DR   OrthoDB; POG091H02C5; -.
DR   Proteomes; UP000010386; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
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   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 membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010386};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010386};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM      7     25       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    294    312       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    317    337       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    343    364       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    385    411       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    417    440       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   484 AA;  51560 MW;  68F840A7772F7F5D CRC64;
     MPKQSRLLVV ILAIVVGAIF TLITVPPRLG LDLRGGAQLT LQALPAPQRG INSINAQLLE
     SARFAIEQRV NSLGVSEATV LTSGDDQLVV QLPGVSDPDQ AERVLGRTAL LEFRKQRQGS
     EGIIAAERQV QSDLFLELQQ LDPSDEAAIA ENQAAMERSR QRVNDLFEST GLTGDSLTNA
     LASPIGQGVW YVSLRFDSEG AQKFAEITGE LGGTGRGLGI FLDDDLVSAP QVNAEFQGTG
     ITGGQAAIEG SFSQEQAIEL ALQLRAGALP VPVEIVENRT VGATLGADSV RSSIYAGFGG
     LILVLLFMVV YYRLPGFVAD IALVIYSLIT LALYSLFGVT LTLPGIAGFI LSIGIAVDAN
     ILIFERTREE LIAGRTVYKS VEAGFGRAWS SILDSNITTL IACGALFWFG ASLVKGFAVT
     LSLGVLVSMF TAVTFSRSLL LSIISDPRFR KPELYGIKSI PKPTAKSKKN QSSDKTDKPK
     GASL
//
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