ID A0A0Q9YLZ4_9COXI Unreviewed; 620 AA.
AC A0A0Q9YLZ4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=CC99x_01743 {ECO:0000313|EMBL:KRG18298.1};
OS Candidatus Berkiella cookevillensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Berkiella.
OX NCBI_TaxID=437022 {ECO:0000313|EMBL:KRG18298.1, ECO:0000313|Proteomes:UP000051494};
RN [1] {ECO:0000313|EMBL:KRG18298.1, ECO:0000313|Proteomes:UP000051494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC99 {ECO:0000313|EMBL:KRG18298.1,
RC ECO:0000313|Proteomes:UP000051494};
RA Mehari Y.T., Arivett B.A., Farone A.L., Gunderson J.H., Farone M.B.;
RT "Draft Genome Sequences of Two Novel Amoeba-resistant Intranuclear
RT Bacteria, Candidatus Berkiella cookevillensis and Candidatus Berkiella
RT aquae.";
RL Submitted (SEP-2015) 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}.
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:KRG18298.1}.
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DR EMBL; LKHV01000008; KRG18298.1; -; Genomic_DNA.
DR RefSeq; WP_057624820.1; NZ_LKHV02000001.1.
DR AlphaFoldDB; A0A0Q9YLZ4; -.
DR STRING; 437022.CC99x_01743; -.
DR PATRIC; fig|1590042.3.peg.1771; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000051494; 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; 3.30.70.260; -; 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; IPR001036; Acrflvin-R.
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 PRINTS; PR00702; ACRIFLAVINRP.
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:UP000051494};
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 459..478
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 485..504
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 510..531
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 552..572
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 578..598
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 2..103
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 231..288
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 437..598
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 620 AA; 67366 MW; 9301E26901437D1A CRC64;
MLNKYPLWKY LLLLGILLVG LVYALPNLFG EDPAVQVLAS TGSSLDPSII EKIEDHLKEK
DIPYISIKHE NSTILTRFST PQIQLQAKEA IKEVVGENYI VALNLAPKTP AWLTWFGASP
MKLGLDLRGG VHFLMEVDVE SSFSRYLESA LGEIRSLMRE NKLRYSQLYK VDNDKLVVVS
FDSEAGAKDA LKIINQHFKD YDFIQKKVDN RYQLLGHIKQ VSVQEITNST VEKSISTLRN
RVNELGVSEA VVQRQGLNHI IVELPGIQDT ARAKDILGKT ATLAFHLEAT EEAKKATPNI
TPPGTKWYTD RGNRQVLLSK RVILTGDSII GAVVGSDGQT GQPAVHVTVA NKGLALWQKT
TLENVGVGLG VVYIETKTDS VEENGESVKK TWTSENLISF ATIRSPLGNR FQITGFTLQQ
AQDLAILLRA GSLPATITIV EERTVGPSLG QENIRLGKLS IAVGLGLVVV AMLLYYSVFG
FIANLALVAN VILLVAILSL VGATLTLPGI AGIVLTIGMA VDANVLIFER IREELRLGLS
AQAAIHAGFE RALSTIIDAN LTTLIVAVIL FSVGTGPIRG FAITLTIGIL TSMLTAIMGT
RAMVNIAYGG RTVQKLRVGI
//
