ID A0A448PC00_9ACTO Unreviewed; 637 AA.
AC A0A448PC00;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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:VEI12478.1};
GN ORFNames=NCTC13354_00157 {ECO:0000313|EMBL:VEI12478.1};
OS Trueperella bialowiezensis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Trueperella.
OX NCBI_TaxID=312285 {ECO:0000313|EMBL:VEI12478.1, ECO:0000313|Proteomes:UP000269542};
RN [1] {ECO:0000313|EMBL:VEI12478.1, ECO:0000313|Proteomes:UP000269542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13354 {ECO:0000313|EMBL:VEI12478.1,
RC ECO:0000313|Proteomes:UP000269542};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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. Other proteins may also be involved.
CC {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; LR134476; VEI12478.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A448PC00; -.
DR KEGG; tbw:NCTC13354_00157; -.
DR Proteomes; UP000269542; Chromosome 1.
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; 3.30.70.3220; -; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR HAMAP; MF_01463_B; SecD_B; 1.
DR InterPro; IPR004869; MMPL_dom.
DR InterPro; IPR005791; SecD.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR048631; SecD_1st.
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; PF03176; MMPL; 1.
DR Pfam; PF21760; SecD_1st; 1.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01463};
KW Protein transport {ECO:0000256|HAMAP-Rule:MF_01463};
KW Reference proteome {ECO:0000313|Proteomes:UP000269542};
KW Translocation {ECO:0000256|HAMAP-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}; Transport {ECO:0000256|HAMAP-Rule:MF_01463}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 397..419
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 425..448
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 476..495
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 501..528
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 76..129
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 375..565
FT /note="Membrane transport protein MMPL"
FT /evidence="ECO:0000259|Pfam:PF03176"
FT REGION 591..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 637 AA; 68025 MW; 9C3D332FD3D96E52 CRC64;
MSQSIHDGDS QPRPIRRLIV VALMLAALIG SLVVGTMTTG KSRFTPDLAL DLEGGTQIIL
TPVTTDGSEV TSQDIREAIN IIRQRVDATG VAEAEITAQG GSNIIVSLPG QPSQETLDLV
RTSAVLRMRP SLTILDPGPL TADSVVKALG DKAQGMDPAQ MNDEDLDKAI RQLADVNGDG
ELATEPAQEP ANPSDPAWIT EQLMYEAYKL DCTVPDTRSA AQTDNPNTAI VACDPESQTK
HLLGPAELDG TNLDTASSGP DVNSQGVATG GWAVNMSFDD EGGKIFADVT ARLSGLQYPQ
NAFAAVLDGK VISFATVSSV IPGGEAKISG SFNAKEAANL ANQLKFGSLP LQFEVQSEEQ
ISATLGSEQL VSGLIAGLVG MLLIVGYMIW QYHALGVIAI GSILLSTGMS YLIISLLSWT
MGYRLSMAGV LGIIISIGVT ADSFIVYFER IRDEIRDGRT IPAAVRHGWD RAKRTIIISD
VVNLVAAVVL YLLTVGSVRG FAFTLGITTV LDLFVVTMFT YPLMTLIAKT EFFGKGKRGS
GMDPIKLEAL PRYRGRGVAS RSTPKRSAAK KRSLVTSDGV ELHDYELPDA RFTDAGAPGF
RQSRREEELG SGESLAKRRA RERRQARKAQ AAEGDEA
//
