ID A0A5B8RTU3_9BURK Unreviewed; 633 AA.
AC A0A5B8RTU3;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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:QEA12533.1};
GN ORFNames=FOZ74_05535 {ECO:0000313|EMBL:QEA12533.1};
OS Comamonas flocculans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=2597701 {ECO:0000313|EMBL:QEA12533.1, ECO:0000313|Proteomes:UP000321199};
RN [1] {ECO:0000313|EMBL:QEA12533.1, ECO:0000313|Proteomes:UP000321199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NLF 7-7 {ECO:0000313|EMBL:QEA12533.1,
RC ECO:0000313|Proteomes:UP000321199};
RA Kim D.H., Kim J.G.;
RT "Complete genome sequence of Comamonas sp. NLF 7-7 isolated from
RT livestock.";
RL Submitted (JUL-2019) 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; CP042344; QEA12533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B8RTU3; -.
DR KEGG; cof:FOZ74_05535; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000321199; 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:UP000321199};
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..470
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 477..495
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 544..566
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 572..600
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 1..108
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 235..293
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 429..599
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 633 AA; 68134 MW; 4875F2591786B261 CRC64;
MNRYPAWKYV IIAVALLVAA LYTLPNFYGE APAVQVSSAK ATIKIDAAVL ERVQQAIQAA
GLKSDSVVLE GSSVRARFDT PDDQLKAKDA IEKALIPDPS DPPYIVALNL VSRSPDWLTA
INARPMYLGL DLRGGVHFML QVDMQAALTK KAESYAGDLR TSLREKGIRH GGISREGQSI
RVRLRDDAAV AAARNLVGDQ FPDLQVAVAP DGEAQLLTAT IKPESLRKVQ EQALKQNIVT
LHNRINELGV AEPVIQQQGL DRIVVQLPGV QDTAKAKDIL GRTATLEVRM VDESTEGRAA
EMGTGPVPFG DEKYLDRNQQ AVIVKKQVIL TGENLTDAQP GFDGQTQEPT VNLTLDAKGS
RIFKDVTREN VGKRMAIVLF EKGKGEVVTA PVIRTEIGGG RVQISGRMTT VEANDTALLL
RAGSLAAPME IIEEYTIGPS LGADNIQRGI HSVVWGMAVI AAFMCIYYLL FGVFSTLALS
VNVLLLIAVL SMLQATLTLP GIAAMALALG VAIDSNVLIN ERIREELRAG VAPQSAIHAG
YENAWATILD SNVTTLIAGL ALLAFGSGPV RGFAVVHCIG ILTSMFSAVF FSRGVVNLWY
GKKKKLKSIS IGQIWKPEDG SELRSVAGRG YNN
//
