ID A0A1J4QKC3_9GAMM Unreviewed; 617 AA.
AC A0A1J4QKC3;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-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 ORFNames=BFR47_07945 {ECO:0000313|EMBL:OIN14414.1};
OS Oceanisphaera psychrotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Oceanisphaera.
OX NCBI_TaxID=1414654 {ECO:0000313|EMBL:OIN14414.1, ECO:0000313|Proteomes:UP000243073};
RN [1] {ECO:0000313|EMBL:OIN14414.1, ECO:0000313|Proteomes:UP000243073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAM-WHM-ZC {ECO:0000313|EMBL:OIN14414.1,
RC ECO:0000313|Proteomes:UP000243073};
RA Zhuo S., Ruan Z.;
RT "Draft Genome Sequence of Oceanisphaera psychrotolerans, isolated from
RT coastal sediment samples.";
RL Submitted (JUL-2016) 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: 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:OIN14414.1}.
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DR EMBL; MDKE01000001; OIN14414.1; -; Genomic_DNA.
DR RefSeq; WP_071471217.1; NZ_MDKE01000001.1.
DR AlphaFoldDB; A0A1J4QKC3; -.
DR STRING; 1414654.BFR47_07945; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000243073; 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; 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};
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 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 505..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..607
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..597
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 617 AA; 67029 MW; B246D868B56FA520 CRC64;
MLNRYPLWKY LMVIAVITIS FLYAAPNLFG EDPALQVSGS RGTQVTPAVL NQAQQTLSNA
GIAVKSAALA DDQLLIRFRN TDDQLKGKDL VADVLGDGYI TALNLAPSTP SWLEAIGAGP
LKLGLDLRGG VHFLMEVDMD EALSRVQEQT VQDFRTDLRE QRLRYSGVLA KDGGTLVVFR
DAETRDQALS HLRGRYPGLV FSDRDNGETF GLFAMMSEQR LKEVKEYALQ QNITIIRNRV
NELGVAEPLV QRQGAERIVV QLPGIQDTAR AKEILGATAT LEFRLVDESA DVAAASAGRV
PPNSELMRDR DGRPVVLQKR IILTGEHIVD ASSGMDEFSR PQVNISLDAP GGSRMADFTK
DNVGRPMATV FTEYKPGDEQ NEDGTRQFRK QQEVINVATI QSRLGRSFRI TGIDSMAEAQ
NLALLLRAGA LIAPIQIVEE RTIGPSLGQQ NVENGLLAMV YGMLAVVLFM LIYYRKFGLV
ANAALLANLV IIIGVMSMVP GATMTLPGIA GIVLTIGMSV DANVLIFERI REELRDGRGV
QQAIHIGYDK ALGTIADANI TTLLTAIILF AVGTGPIKGF AVTLMIGILA SMFTAIVGTR
ALVNLLWGGK RLSKLSI
//
