ID T0PAJ1_AERSA Unreviewed; 617 AA.
AC T0PAJ1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD1 {ECO:0000313|EMBL:ATP09113.1};
GN Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=Asalp_19100 {ECO:0000313|EMBL:ATP09113.1};
OS Aeromonas salmonicida subsp. pectinolytica 34mel.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1324960 {ECO:0000313|EMBL:ATP09113.1, ECO:0000313|Proteomes:UP000222916};
RN [1] {ECO:0000313|Proteomes:UP000222916}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=34mel {ECO:0000313|Proteomes:UP000222916};
RX PubMed=29304740; DOI=10.1186/s12864-017-4301-6;
RA Pfeiffer F., Zamora-Lagos M.A., Blettinger M., Yeroslaviz A., Dahl A.,
RA Gruber S., Habermann B.H.;
RT "The complete and fully assembled genome sequence of Aeromonas salmonicida
RT subsp. pectinolytica and its comparative analysis with other Aeromonas
RT species: investigation of the mobilome in environmental and pathogenic
RT strains.";
RL BMC Genomics 19:20-20(2018).
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}.
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DR EMBL; CP022426; ATP09113.1; -; Genomic_DNA.
DR RefSeq; WP_021139833.1; NZ_CP022426.1.
DR AlphaFoldDB; T0PAJ1; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000222916; 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; 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};
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 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 458..476
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 509..530
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 551..573
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 579..603
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 229..288
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 435..603
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 617 AA; 67528 MW; 91E286B573AB2B85 CRC64;
MLNRYPLWKY LMVVFVIAIG FLYAAPNLYG EDPALQVSAS RGAEVKLDTL DLVKETLEAA
SIPVKHAAFE HGLILVRFQN TEDQLKARDL VANKLGDNFI TALNLAPSTP AWLEAIGAAP
LKLGLDLRGG VHFLMEVDMA EALTKQQEQM VQDFRTELRT QKIRYSGVRR VGDQVQVLFR
DEADQERAVS YLRRQNPDLT FTTEQKGDEF VLNAALSDAK IKEVRKYALE QNITIIRNRV
NELGVAEPLV QQQGAERIVV QLPGIQDTAR AKEILGATAT LEFHMVDETA DIQAAADGRV
PPSSKVYNDR NGRPVVLQKR VILTGDHIVG AQSGFDEYSR PQVNIKLDGQ GGNKMANFTK
DNVGKGMATV FIEYKPVGQP GPDGKRKFRK QEEVINVATI QSRLGSQFRI TGIDNANEAH
NLALLLRAGA LIAPIQIVEE RTIGPSLGQQ NIDSGMEAIG WAMLVIVLFM GIYYRAFGWV
ANLALTMNLV LIVGIMSMIP GATMTLPGIA GIVLTLGMAV DANVLIYERI REEIRNGRGV
QQAIHLGFDR AFSTIADSNV TSLITCVILF GIGTGAIKGF ALTLGIGLSA SMFTAITVSR
AIINLGWGGR RIDKLPI
//
