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Database: UniProt
Entry: E0UPP1_SULAO
LinkDB: E0UPP1_SULAO
Original site: E0UPP1_SULAO 
ID   E0UPP1_SULAO            Unreviewed;       521 AA.
AC   E0UPP1;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   OrderedLocusNames=Saut_0584 {ECO:0000313|EMBL:ADN08633.1};
OS   Sulfurimonas autotrophica (strain ATCC BAA-671 / DSM 16294 / JCM 11897 /
OS   OK10).
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurimonadaceae; Sulfurimonas.
OX   NCBI_TaxID=563040 {ECO:0000313|EMBL:ADN08633.1, ECO:0000313|Proteomes:UP000007803};
RN   [1] {ECO:0000313|EMBL:ADN08633.1, ECO:0000313|Proteomes:UP000007803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC   {ECO:0000313|Proteomes:UP000007803};
RX   PubMed=21304749;
RA   Sikorski J., Munk C., Lapidus A., Ngatchou Djao O.D., Lucas S.,
RA   Glavina Del Rio T., Nolan M., Tice H., Han C., Cheng J.F., Tapia R.,
RA   Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Sims D., Meincke L., Brettin T., Detter J.C.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Rohde M., Lang E., Spring S., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Sulfurimonas autotrophica type strain
RT   (OK10).";
RL   Stand. Genomic Sci. 3:194-202(2010).
RN   [2] {ECO:0000313|Proteomes:UP000007803}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-671 / DSM 16294 / JCM 11897 / OK10
RC   {ECO:0000313|Proteomes:UP000007803};
RX   DOI=10.4056/sigs.1173118;
RA   Sikorski J., Munk C., Lapidus A., Djao O., Lucas S., Glavina Del Rio T.,
RA   Nolan M., Tice H., Han C., Cheng J., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Sims D.,
RA   Meincke L., Brettin T., Detter J., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y., Jeffries C., Rohde M., Lang E., Spring S., Goker M.,
RA   Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P., Kyrpides N.,
RA   Klenk H.;
RT   "Complete genome sequence of Sulfurimonas autotrophica type strain
RT   (OK10T).";
RL   Stand. Genomic Sci. 3:194-202(2010).
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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP002205; ADN08633.1; -; Genomic_DNA.
DR   RefSeq; WP_013326389.1; NC_014506.1.
DR   AlphaFoldDB; E0UPP1; -.
DR   STRING; 563040.Saut_0584; -.
DR   KEGG; sua:Saut_0584; -.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_4_3_7; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000007803; Chromosome.
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   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; 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; PF21760; SecD_1st; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
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}; Reference proteome {ECO:0000313|Proteomes:UP000007803};
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        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        352..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        378..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        405..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        448..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        476..500
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          137..199
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          337..504
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   521 AA;  56425 MW;  6D7DF1B8293ADE24 CRC64;
     MKLNYRIVIF ALAIVFGIVF SLPSLLQTQS GKKITLGLDL QGGLHMLLGV KTEEATKSRI
     KSMAASIKHF AERNDILING LTFDNKSVTF EVLDSDEIKT FDEFLSKLEG VTVTHKGSVI
     SVSLTPKEIE KTKKQAVSQA IETIRNRLDQ FGLSEPIVAR QGKDKILVEL AGIKSQEDEQ
     RARELISRAA KLELMAVDED RNARVYNMSD ADAASYGDII LEDVKSPKIK YLVHEIPILD
     GGMLTGANVG FDQNNRPVIN FKLNAEGADI FGDFTGKNVG KRLAVVLDGK VYSAPNINER
     IGGGSGQISG NYTVLEAKDL AIALRSGALL APIYLMEKRS VGPSLGADSI KASMIALIGG
     FVLVIVFMMV YYRMAGVIAN IALIANLLLL LAVMSLFGAT LTLPGMAGIV LTVGMAVDAN
     VIITERIREL IYEGKSMHKA IEEGYSNAMR AILDANITTL IASVVLYVYG TGAIKGFAVT
     MSIGILASML TAILGTHGIY QMLESKMGKS KNYRFWFGIK G
//
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