ID A0A0Q4MFW1_9GAMM Unreviewed; 428 AA.
AC A0A0Q4MFW1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Colicin V secretion protein CvaA {ECO:0000313|EMBL:KQN53434.1};
GN ORFNames=ASF13_14815 {ECO:0000313|EMBL:KQN53434.1};
OS Erwinia sp. Leaf53.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN53434.1, ECO:0000313|Proteomes:UP000050856};
RN [1] {ECO:0000313|EMBL:KQN53434.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN53434.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQN53434.1, ECO:0000313|Proteomes:UP000050856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf53 {ECO:0000313|EMBL:KQN53434.1,
RC ECO:0000313|Proteomes:UP000050856};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477}.
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:KQN53434.1}.
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DR EMBL; LMLK01000026; KQN53434.1; -; Genomic_DNA.
DR RefSeq; WP_056241312.1; NZ_LMLK01000026.1.
DR AlphaFoldDB; A0A0Q4MFW1; -.
DR STRING; 1736225.ASF13_14815; -.
DR Proteomes; UP000050856; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR Gene3D; 2.40.50.100; -; 1.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006144; Secretion_HlyD_CS.
DR PANTHER; PTHR30386:SF27; EXPORTED PROTEIN-RELATED; 1.
DR PANTHER; PTHR30386; MEMBRANE FUSION SUBUNIT OF EMRAB-TOLC MULTIDRUG EFFLUX PUMP; 1.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR Pfam; PF13437; HlyD_3; 1.
DR PRINTS; PR01490; RTXTOXIND.
DR PROSITE; PS00543; HLYD_FAMILY; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000050856};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 68..103
FT /note="Membrane fusion protein biotin-lipoyl like"
FT /evidence="ECO:0000259|Pfam:PF13533"
FT COILED 115..160
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 428 AA; 47428 MW; C2FA8A94DDB58A26 CRC64;
MPIQFRPEVT QHQQSRWNGQ VLLLNGWPLW LTLLLTAGFI IALLTLLISG TYTRRITVNG
EIITEPRTIN LFAPEQGIVS KLLVADGQQV NAGTPLYQLD VSQVTDTGSV SGTTLTILEQ
QTKQLDAIIS QLQSNKRETL SSLQQQLKQY QQAQQGLEGM VTTAREGLQA MRASRDSYEA
SLRKGLINTD QMNNQRYLYY QQQSVFQSLN SQALQQSLQI TTLKSELQTK AADFDNQIAQ
SRYQRDDLAR QRAETGARGS RMIIAPTRGV VSSLSVTPGQ MVNAGDSLIQ LVPSSHASVL
FVAWLPDDSR PHVAPGETIN IRYAAFPYEK YGQFPGRIVS VSAAPVPVRE LEGWASVPRD
PAGRVNGSWY KATVALDNGG LSWQGQPLVL SSGMQAQSTL FLEKRPLYQW MLSPYYSLKK
SITGPVNE
//
