ID K0CEA6_ALCDB Unreviewed; 627 AA.
AC K0CEA6;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463,
GN ECO:0000313|EMBL:AFT71939.1};
GN OrderedLocusNames=B5T_03675 {ECO:0000313|EMBL:AFT71939.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT71939.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT71939.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(2012).
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-YajC and YidC. {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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR EMBL; CP003466; AFT71939.1; -; Genomic_DNA.
DR AlphaFoldDB; K0CEA6; -.
DR STRING; 930169.B5T_03675; -.
DR KEGG; adi:B5T_03675; -.
DR PATRIC; fig|930169.3.peg.3627; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_6; -.
DR Proteomes; UP000006286; 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; -; 2.
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; IPR027398; SecD-TM.
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:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF13721; SecD-TM1; 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 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:UP000006286};
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 463..482
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 513..535
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 556..581
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 587..611
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 1..104
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 228..287
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 443..604
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 627 AA; 67766 MW; 7D2163B53A9BB6D4 CRC64;
MTRYPRWKFF LLMAVLFVCG LYALPNLFPD APAVQISSAK PGGTVSDSAS QRVLRQLDQA
GLEHGPGEQI DGGSWLVRFT DNDSQLRARE LLAGSLGDDY VVALNLAPTT PGWLRAIGAS
PMNLGLDLRG GVHFLLQVDM EAVVNQRMEA WAGQIKLALK NEGIRYRDVQ QDGQQLRVQF
ANSEDADSAR TLLRNALPEF SLDSDPEQRV LVFNLNPTAL KEMQDYAVDQ NRTALNNRVN
ELGVAEPVVQ RQGADRIVVQ LPGVQDAAQA RRILGRTATL EFRLVNQDYP ASRAATGVAP
PGTEIFPFRS QGDRPVILER SKIATGDEVT NAQMGFDPQN GTPQVNVSLD SAGARRMQRV
TSQNVGNPMA VLFIETKTEM SSRTNENGET EQVPVSTTDR YVINVATIQD TLGSRFRITG
LDSPAEASEL ALLLRAGSLA APVTIIEERT IGPSLGAENI ESGLKSMALG MVLVLVFMLV
WYKVFGIFAN VALVGNLLII VGIMSLIPGA TLTLPGIAGI VLTVGMAVDA NVLIYERIRE
ELKKGVRPRQ AIDEGYAKAF STILDANITT MIVAVILFSA GTGSVQGFAV TLFIGILSSM
FTAIVGTRAM VEMVYGRGAR PPAKLSI
//
