ID E1Q5F1_HELPP Unreviewed; 525 AA.
AC E1Q5F1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:ADO07774.1};
GN OrderedLocusNames=HPPC_07880 {ECO:0000313|EMBL:ADO07774.1};
OS Helicobacter pylori (strain PeCan4).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=765963 {ECO:0000313|EMBL:ADO07774.1, ECO:0000313|Proteomes:UP000006863};
RN [1] {ECO:0000313|Proteomes:UP000006863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PeCan4 {ECO:0000313|Proteomes:UP000006863};
RA Kersulyte D., Vasquez J., Gilman R.H., Berg D.E.;
RT "Complete genome sequence of Helicobacter pylori strain PeCan4.";
RL Submitted (JUN-2010) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01463}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {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}.
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DR EMBL; CP002074; ADO07774.1; -; Genomic_DNA.
DR RefSeq; WP_000765405.1; NC_014555.1.
DR AlphaFoldDB; E1Q5F1; -.
DR KEGG; hpc:HPPC_07880; -.
DR HOGENOM; CLU_007894_4_3_7; -.
DR Proteomes; UP000006863; 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; -; 1.
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; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
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; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
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 356..374
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 381..401
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 407..425
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 478..502
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 142..202
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 334..501
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 525 AA; 56739 MW; 6DB0DF2EB2E9D784 CRC64;
MKLFNPRLIV FICALLLGVG FSVPSLLETK GPKITLGLDL RGGLNMLLGV QTDEALKNKY
LSLASALEYN AKKQNILLKD IKSSLEGISF ELLDEDEAKK LDALLLELQG HSQFEIKKEA
EFYSVKLTPL EQEELRKNTI LQVIGIIRNR LDQFGLAEPV VIQQGKEEIS VQLPGIKTLE
EERRAKDLIS RSAHLQMMAV DEEHNKDAMK MTDLEAQKLG SVLLSDVEMG GKILLKAIPI
LDGEMLTDAK VVYDQNNQPV VSFTLDAQGA KIFGDFSGAN VGKRMAIVLD NKVYSAPVIR
ERIGGGSGQI SGNFSVAQAS DLAIALRSGA MSAPIQVLEK RIIGPSLGKD SIKTSIIALI
GGFILVMGFM VLYYSMAGVI ACLALVVNLF LIVAVMAIFG ATLTLPGMAG IVLTVGIAVD
ANIIINERIR EVLRENEGIA KAIHLGYINA SRAIFDSNTT SLIASVLLYA YGTGAIKGFA
LTTGIGILAS IITAIIGTQG IYQALLPKLT QTKSLYFWFG VNKRA
//
