ID A0A1S8CTJ1_9GAMM Unreviewed; 622 AA.
AC A0A1S8CTJ1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=BKE30_10340 {ECO:0000313|EMBL:ONG39159.1};
OS Alkanindiges hydrocarboniclasticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Alkanindiges.
OX NCBI_TaxID=1907941 {ECO:0000313|EMBL:ONG39159.1, ECO:0000313|Proteomes:UP000192132};
RN [1] {ECO:0000313|EMBL:ONG39159.1, ECO:0000313|Proteomes:UP000192132}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|EMBL:ONG39159.1,
RC ECO:0000313|Proteomes:UP000192132};
RA Subhash Y., Lee S.;
RT "Draft Genome sequence of Alkanindiges sp. strain H1.";
RL Submitted (OCT-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: 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:ONG39159.1}.
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DR EMBL; MLCN01000027; ONG39159.1; -; Genomic_DNA.
DR RefSeq; WP_076878530.1; NZ_MLCN01000027.1.
DR AlphaFoldDB; A0A1S8CTJ1; -.
DR STRING; 1907941.BKE30_10340; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000192132; 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; 3.30.70.3400; -; 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 461..480
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 485..507
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 513..535
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 556..578
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 584..608
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 2..102
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 228..286
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 444..611
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 622 AA; 67842 MW; 5C50EFBA6E097E51 CRC64;
MRYPAWKYVL ILFVLVISTL YALPSLYPDE PAVQISGAKA GSQIDQTVLN RAEQILKSAN
IATHNGSFGQ NAALLRLRTS EDQIKAQEIL RRGLGENYVV ALNLAPTTPA WLQAIGAKPM
KLGLDLRGGV HFLLEVDMSK ALEQRLETAT ADIRRNLRDN KVSFNGVRQT KDNIVVNFAT
TTDRDNALSV LRRQSNDFNI QPLASADGPI LQLQYTEARL QEINQYAVNQ NLTTLRNRIN
ELGVAEALVQ TQGSNRIVVD LPGVQDTAEA KRVLGRTANL EFRLVSEQAD TYAGGPVPAG
TQAFPFEKLD GPTILLKRQR IVTGERVQNA MSGYDENNQP EVNITLDTAG GKLMADATRN
AVGKQMAVLF IENKQRISYV TDPVTGKTVE TRTPYTESIV INRATIQAVL GSQFRITGVG
TPQEASELAL LLRAGALAAP MYFVEERTVG PSLGQDNIDK GLLSTQVGFV LVALFMIVFY
RVFGLIANVA LFMNLAMILT IMSWIGAALS LPGIAGIVLT IGMAVDANVL ICERIREEIR
WGSSPKQAIV AGYDRAYTTI FDSNLTTLLV AFILFAIGSG PIKGFAVTLA IGIICSMFTA
ITVTRGIVQL VYGKRRIEKL SI
//