ID L5N1V9_9BACI Unreviewed; 533 AA.
AC L5N1V9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=D479_17559 {ECO:0000313|EMBL:ELK44804.1};
OS Halobacillus sp. BAB-2008.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=1246484 {ECO:0000313|EMBL:ELK44804.1, ECO:0000313|Proteomes:UP000010769};
RN [1] {ECO:0000313|EMBL:ELK44804.1, ECO:0000313|Proteomes:UP000010769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-2008 {ECO:0000313|EMBL:ELK44804.1,
RC ECO:0000313|Proteomes:UP000010769};
RX PubMed=23469348;
RA Joshi M.N., Pandit A.S., Sharma A., Pandya R.V., Saxena A.K.,
RA Bagatharia S.B.;
RT "Draft Genome Sequence of the Halophilic Bacterium Halobacillus sp. Strain
RT BAB-2008.";
RL Genome Announc. 1:E00222-12(2013).
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 membrane {ECO:0000256|HAMAP-Rule:MF_01463};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01463}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01463}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELK44804.1}.
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DR EMBL; ANPF01000083; ELK44804.1; -; Genomic_DNA.
DR AlphaFoldDB; L5N1V9; -.
DR PATRIC; fig|1246484.3.peg.3573; -.
DR eggNOG; COG0342; Bacteria.
DR Proteomes; UP000010769; Unassembled WGS sequence.
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; 3.30.70.3220; -; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
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 InterPro; IPR048631; SecD_1st.
DR InterPro; IPR048634; SecD_SecF_C.
DR NCBIfam; TIGR00916; 2A0604s01; 1.
DR NCBIfam; TIGR01129; secD; 1.
DR PANTHER; PTHR30081:SF8; PROTEIN TRANSLOCASE SUBUNIT SECF; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF21760; SecD_1st; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE 3: Inferred from homology;
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:UP000010769};
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 269..287
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 292..309
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 363..384
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 396..419
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 63..120
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 247..410
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 533 AA; 58583 MW; 709A01BD72D6C768 CRC64;
MVKRGRIVAF FLVVLLIASA IGTTITGITK DIKLGLDLQG GFEILYDVEP LNEDQEVNDQ
VLEATAESLN QRVNTLGISE TNISIEDGGR IRVQLAGVED QQTARELLST SAQLSMRGTD
GKEYLNGSDL VEGSAQQTFN PDTNEPVVTL KVKDASKFYD VSKEIYETPD DPETPYPDDL
LVIWLDYNED TSFAEEYGKE DPGYISAPSF RQNGPIRSNS IMISGDFTVE SAKQLADVLN
AGSLPVNLEE TYSTSVGAQF GEQAMNKTIL AGFIGVAVIF LFMIAYYRFP GVIATITLTT
YIYLILLVFE WMNGVLTLPG IAALILGVGM AVDANIITYE RIKEELKSGK SLMSAYKAGN
KRSLSTILDA NITTLIAAAV LFIFGTSSVK GFATMLIVSI LVSFITAVYG TRLFMGLWVK
SRFLNKRPKW FGVKPEDIQN IEDGQEVEAT FAKRQFDFVG LRKRFFAVSI ALVVAGIIAI
AIFRLNLGID FTSGSRVSIL ADENVSSEQI EQTMEDEFDL SPKKSLFPEI ITK
//
