ID A0A0H4WEI4_9BORD Unreviewed; 311 AA.
AC A0A0H4WEI4;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN Name=secF {ECO:0000256|HAMAP-Rule:MF_01464,
GN ECO:0000313|EMBL:AZW15442.1};
GN ORFNames=ACR54_01476 {ECO:0000313|EMBL:AKQ54801.1}, CS347_00830
GN {ECO:0000313|EMBL:AZW15442.1};
OS Bordetella hinzii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=103855 {ECO:0000313|EMBL:AKQ54801.1, ECO:0000313|Proteomes:UP000036382};
RN [1] {ECO:0000313|EMBL:AKQ54801.1, ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|EMBL:AKQ54801.1,
RC ECO:0000313|Proteomes:UP000036382};
RX PubMed=26316634;
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Strains Isolated from
RT Humans.";
RL Genome Announc. 3:e00965-e00915(2015).
RN [2] {ECO:0000313|Proteomes:UP000036382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F582 {ECO:0000313|Proteomes:UP000036382};
RA Weigand M.R., Changayil S., Kulasekarapandian Y., Batra D., Williams M.M.,
RA Tondella M.L.;
RT "Complete Genome Sequences of Two Bordetella hinzii Isolated from Humans.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000282741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H720 {ECO:0000313|Proteomes:UP000282741};
RA Weigand M.R., Loparev V., Peng Y., Bowden K.E., Tondella M.L.,
RA Williams M.M.;
RT "Whole genome sequencing of various Bordetella species.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AZW15442.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H720 {ECO:0000313|EMBL:AZW15442.1};
RX PubMed=31744907;
RA Weigand M.R., Peng Y., Batra D., Burroughs M., Davis J.K., Knipe K.,
RA Loparev V.N., Johnson T., Juieng P., Rowe L.A., Sheth M., Tang K.,
RA Unoarumhi Y., Williams M.M., Tondella M.L.;
RT "Conserved Patterns of Symmetric Inversion in the Genome Evolution of
RT Bordetella Respiratory Pathogens.";
RL mSystems 4:e00702-19(2019).
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_01464}.
CC -!- SUBUNIT: Forms a complex with SecD. 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_01464}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01464}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01464}.
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DR EMBL; CP012076; AKQ54801.1; -; Genomic_DNA.
DR EMBL; CP024172; AZW15442.1; -; Genomic_DNA.
DR RefSeq; WP_029579456.1; NZ_LT906461.1.
DR STRING; 103855.ACR54_01476; -.
DR GeneID; 56618680; -.
DR KEGG; bhz:ACR54_01476; -.
DR PATRIC; fig|103855.14.peg.1415; -.
DR eggNOG; COG0341; Bacteria.
DR OrthoDB; 9774769at2; -.
DR Proteomes; UP000036382; Chromosome.
DR Proteomes; UP000282741; 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; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR HAMAP; MF_01464_B; SecF_B; 1.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR022646; SecD/SecF_CS.
DR InterPro; IPR048634; SecD_SecF_C.
DR InterPro; IPR005665; SecF_bac.
DR NCBIfam; TIGR00916; 2A0604s01; 1.
DR NCBIfam; TIGR00966; transloc_SecF; 1.
DR PANTHER; PTHR30081:SF8; PROTEIN TRANSLOCASE SUBUNIT SECF; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR01755; SECFTRNLCASE.
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_01464};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01464};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01464}; Reference proteome {ECO:0000313|Proteomes:UP000036382};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01464}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 133..154
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 161..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 188..209
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 248..266
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT DOMAIN 107..291
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 311 AA; 34640 MW; 9C8A989D4895BC5D CRC64;
MEFFRIHRTI PFMRHALVLN IISLVTFIAA VFFIITRGFH LSIEFTGGTV MEVNYAQTAQ
LDQVRGVVGK LGYSDFQVQN FGTSRDVMIR LPLAEGQTSA TQSETVMAAL KAADASVELR
RVEFVGPQVG QELLHNGLMA LLVVVIGIMI YLGFRFEWKF AVAGVIANLH DVVIILGFFA
FFQWEFSLSV LAGVLAVLGY SVNESVVIMD RIRENFRKYR KADVQEVINS AITQTISRTI
ITHGSTQMMV LAMLFFGGPT LHYFALALTI GIWFGIYSSV FVAAALAMWL GVKREDLVKP
VKKAEDEVEV P
//
