ID A0A222FK70_9GAMM Unreviewed; 619 AA.
AC A0A222FK70;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:ASP39425.1};
GN ORFNames=CHH28_12410 {ECO:0000313|EMBL:ASP39425.1};
OS Bacterioplanes sanyensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Bacterioplanes.
OX NCBI_TaxID=1249553 {ECO:0000313|EMBL:ASP39425.1, ECO:0000313|Proteomes:UP000202440};
RN [1] {ECO:0000313|EMBL:ASP39425.1, ECO:0000313|Proteomes:UP000202440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NV9 {ECO:0000313|EMBL:ASP39425.1,
RC ECO:0000313|Proteomes:UP000202440};
RA Rehman Z.U.;
RT "Annotated genome sequence of Bacterioplanes sanyensis isolated from Red
RT Sea.";
RL Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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; CP022530; ASP39425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222FK70; -.
DR KEGG; bsan:CHH28_12410; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000202440; 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 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:UP000202440};
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 453..473
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 480..500
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 506..528
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 549..571
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 577..599
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 2..104
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 230..288
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 437..602
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 619 AA; 68097 MW; 07A0BA073D9AD7BE CRC64;
MLNKYPLWKN LLIVLVVVIS AIYAAPNLYP PDPAIQVTPS QAGAEMSEAT LAKVRAAMTD
AKLDFFGEEV IDGTALFRLQ QTSDQLPAKA AVQRALGDDY VVALNLAPTT PDWLLSLGAG
PMTLGLDLSG GVHFLMEVDM EEYMAGKVSN YRQELRTRLR QEDLRYRRIQ VEGDYLRISF
EDEATRDTAE NFFIREFPEF SRTTEEVAEF YDLKLRMTEQ QIKTYEDYAV KQNLSTLRNR
VNELGVAEPL VQRQGRNRIV VQLPGVQDTA EAKKILGKAA NLEFRLEAEP GANRFTTEEY
PFRSEAFRTA RLEKAVITTG DSVTNARSAF DENGMPQVNI DLDAKGGARM TQVTRKAVQR
RMAVLFVERK PRTTYEMVDG EEVVKTVQVT EKSIISLATI QTTLGSSFRI TGLQAAEASE
LALLLRSGAL AAPMYFVEER TVGPSLGKEN IEMGVQSVMV GLALVLVAML VFYRAFGLMA
NISLMVNIVM LVALMSIVGA TLTLPGIAGI VLTVGMAVDA NVLIFARIRE ELKNGRSPQQ
AIHEGYSRAF VTIFDANLTT LLVAVILFAA GTGPVKGFAV TLSFGILTSM FTAIVLNRAM
VNLVYGGRRV ESLAIGGRV
//
