ID B6BWI8_9PROT Unreviewed; 630 AA.
AC B6BWI8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 24-JAN-2024, entry version 63.
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:EDZ64254.1};
GN ORFNames=KB13_386 {ECO:0000313|EMBL:EDZ64254.1};
OS beta proteobacterium KB13.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales; OM43 clade.
OX NCBI_TaxID=314607 {ECO:0000313|EMBL:EDZ64254.1, ECO:0000313|Proteomes:UP000004188};
RN [1] {ECO:0000313|Proteomes:UP000004188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB13 {ECO:0000313|Proteomes:UP000004188};
RX PubMed=22675594; DOI=10.4056/sigs.2305090;
RA Huggett M.J., Hayakawa D.H., Rappe M.S.;
RT "Genome sequence of strain HIMB624, a cultured representative from the OM43
RT clade of marine Betaproteobacteria.";
RL Stand. Genomic Sci. 6:11-20(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 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR EMBL; DS995299; EDZ64254.1; -; Genomic_DNA.
DR AlphaFoldDB; B6BWI8; -.
DR STRING; 314607.KB13_386; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_4; -.
DR Proteomes; UP000004188; 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; 3.30.1360.200; -; 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 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};
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 464..481
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 488..506
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 555..577
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 583..607
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 1..103
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 244..303
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 439..610
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 630 AA; 69200 MW; B6BE731538ADD2D7 CRC64;
MNQFSRWKNT LILLIVVFAL FYALPNFFGE APAVQIMPIK SGEKMDPIIA SQSEKILEEN
NITYNGVVLT ENFIKIKLTN NEDQLTSKGL LEDKLGPNFV VALNLLPNSP KWLESIGGQP
MYLGLDLRGG VHFLMQVDLS NIEAKESSGR VNEIRTLLRE NKIRYDQISV EDGSILVQLT
NENDLKKSKS LLLQDDSSFE FSKRINLGGS IGKEKIKEIT DNGTFVLAIE GSQANKEEMT
KFAIKQNLET LNNRINELGV AEPIIQQQGE NRIVVQLPGV QDTAKAKDII GRTALLEMRL
VDDEASPADI DQAIDGNIPF GRDLFYDRNQ NPLLLKKDVI LTGENINNAG PGVDNQTGQS
IVSLNLDSKG ANIFKKITRD NIGKRIAILL IEKDITEIIT APVIKSEIGG GRVQITGMKN
AQEATDVSLL LRAGSLAAPM EIIEERTVGP SMGKENIQRG IQSTFWGFIA VIILISIYYM
LFGLFSSIAL SINLVLLVAL LSTIQATLTL PGLAAMALTV GMAIDSNVLI NERIRDEIRN
GNTPQASIHL GYEKAWGTIL DSNITTLIAG IALFMFGTGP IKGFAVVHVL GILTSMFSAI
LVSRALVNFF YGSKRKIDKL NIGEIYKVNN
//
