ID U4K882_9VIBR Unreviewed; 607 AA.
AC U4K882;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=VIBNI_B1845 {ECO:0000313|EMBL:CCO61567.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO61567.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO61567.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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; FO203527; CCO61567.1; -; Genomic_DNA.
DR RefSeq; WP_022561973.1; NC_022543.1.
DR AlphaFoldDB; U4K882; -.
DR STRING; 28173.VIBNI_B1845; -.
DR KEGG; vni:VIBNI_B1845; -.
DR PATRIC; fig|1260221.3.peg.5419; -.
DR eggNOG; COG0342; Bacteria.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000016895; Chromosome 2.
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:SF13; 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:UP000016895};
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 445..464
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 499..517
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 538..563
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 569..593
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 14..109
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 234..292
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 425..595
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 607 AA; 65649 MW; 197C213A8D824F48 CRC64;
MSSPRTRAKT PERMNHYTIW KYVVLLTAIV LLALSALPSW YGDKPALIID QPKADLSIEQ
VSLELKHHNI PIREITETGN QMVVLLESEH DQANAKAAML PTLGAETQIT LAYQSVAPVW
LTQMGFQPVD LGLDLRGGVQ FLLKVDVDQA LHEKQQTLAD DIRTTARKLH IRGIQISHSV
DHQITVTTQT EDSRSEIGKA IQEAFPQWQQ HGQSNKLVLS MPKQSIDEFA QQTLKQNLTI
LRSRIEELGI TEASVQRQGD DYIRIELPGV QDPSQAKSVI GATASLAFHE VETESSKGRI
FSALDEDGNR VRLVSKPVVK GEHIVDARAG LDEMGRAVVN ISLDLAGGGD ISDFSATHVG
KPMATLFSEY VSDAQGNLSK QDKVISVATI QSQLGTRFQI TGAGSMQDAQ ELALLLRAGS
LTAPVTIVEE QAIGASLGAE NIENGFSALA LGMGLTLAFM AVWYRRLGWV ANLALLSNMV
CLLGLIALIP GAVLTLPGIA GLVLTVGMAV DTNVLIFERI KDKLGEGRSF AQSINLGFNS
AVSTIMDANI TTLITAVVLY AIGNGPVQGF ALTLGLGILT SMFTGIFLSR AIINLIWGQD
ARRDVRV
//
