ID A0A066UER5_9GAMM Unreviewed; 625 AA.
AC A0A066UER5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
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:KDN25921.1};
GN ORFNames=MBO_01965 {ECO:0000313|EMBL:KDN25921.1};
OS Moraxella bovoculi 237.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=743974 {ECO:0000313|EMBL:KDN25921.1, ECO:0000313|Proteomes:UP000035860};
RN [1] {ECO:0000313|EMBL:KDN25921.1, ECO:0000313|Proteomes:UP000035860}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=237 {ECO:0000313|EMBL:KDN25921.1,
RC ECO:0000313|Proteomes:UP000035860};
RX PubMed=24970830;
RA Calcutt M.J., Foecking M.F., Martin N.T., Mhlanga-Mutangadura T.,
RA Reilly T.J.;
RT "Draft Genome Sequence of Moraxella bovoculi Strain 237T (ATCC BAA-1259T)
RT Isolated from a Calf with Infectious Bovine Keratoconjunctivitis.";
RL Genome Announc. 2:e00612-14(2014).
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:KDN25921.1}.
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DR EMBL; AOMT01000005; KDN25921.1; -; Genomic_DNA.
DR RefSeq; WP_036362605.1; NZ_AOMT01000005.1.
DR AlphaFoldDB; A0A066UER5; -.
DR eggNOG; COG0342; Bacteria.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000035860; 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}; Reference proteome {ECO:0000313|Proteomes:UP000035860};
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 462..479
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 512..536
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 557..579
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 585..609
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 230..287
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 445..612
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 625 AA; 67296 MW; 9B5E0D8404820332 CRC64;
MHYPAWKYIL IAVVLVISGL YALPNLYPDE PAVQITGASA GVQLTEDVVN ESQGLLDKAG
LSHHGGSFSN NSALVRLSTA EDQLKAQEVL RRELGENYVV ALNLAQTTPE WLRNIGAKPM
KLGLDLRGGV RFVLEVDMAK ALEQRLATAS QDARRALRAD KIAIKSLRTT EDGMMLVFNG
NDIRDRAQSI LQAQMANEFT LRPLADTEGA ALQLSYTEAR LNEINEYAVG QNLTTLRNRI
NELGVAEALV QSQGANRIVV ELPGVQDTAE AKRVLGRTAN LEFRMVSDDT DSFTGGIAPA
GTEAYPFGDL NGPPILLNRQ PIVTGEKVQG AQAGLDENGR PQVSINLDTQ GGRLMQNATA
PAVGKQMAVL FIENKQRVSY ETDPQTGETT EVRTPYSETR VINRATINAV LGSSFVITGL
DSTAEADELA LLLRSGALAA PMYFVEERTI GPSLGQDNID KGLFASKIGY LLVFLWMIVF
YRACGVIASI ALAFNIVMLA AIMSIIGSSL TLPGIAGVVL TMGMAVDANV LIFERIREEI
DAGARAKSAI VAGFDRAFSS ILDGNMTTLL VAFILFAVGT GPVKGFAITL AIGIITSLFT
AIIVTRALMQ IWYGYRKNLT KISIG
//
