ID A0A1G5NRB5_AFIMA Unreviewed; 199 AA.
AC A0A1G5NRB5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Inner membrane-spanning protein YciB {ECO:0000256|HAMAP-Rule:MF_00189};
GN Name=yciB {ECO:0000256|HAMAP-Rule:MF_00189};
GN ORFNames=SAMN03080610_02492 {ECO:0000313|EMBL:SCZ39694.1};
OS Afifella marina DSM 2698.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Afifellaceae; Afifella.
OX NCBI_TaxID=1120955 {ECO:0000313|EMBL:SCZ39694.1, ECO:0000313|Proteomes:UP000199347};
RN [1] {ECO:0000313|EMBL:SCZ39694.1, ECO:0000313|Proteomes:UP000199347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2698 {ECO:0000313|EMBL:SCZ39694.1,
RC ECO:0000313|Proteomes:UP000199347};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in cell envelope biogenesis, maintenance of cell
CC envelope integrity and membrane homeostasis. {ECO:0000256|HAMAP-
CC Rule:MF_00189}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_00189}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_00189}.
CC -!- SIMILARITY: Belongs to the YciB family. {ECO:0000256|HAMAP-
CC Rule:MF_00189}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMVW01000005; SCZ39694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5NRB5; -.
DR STRING; 1120955.SAMN03080610_02492; -.
DR OrthoDB; 9788219at2; -.
DR Proteomes; UP000199347; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR HAMAP; MF_00189; YciB; 1.
DR InterPro; IPR006008; YciB.
DR NCBIfam; TIGR00997; ispZ; 1.
DR PANTHER; PTHR36917:SF1; INNER MEMBRANE-SPANNING PROTEIN YCIB; 1.
DR PANTHER; PTHR36917; INTRACELLULAR SEPTATION PROTEIN A-RELATED; 1.
DR Pfam; PF04279; IspA; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00189};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00189};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_00189};
KW Reference proteome {ECO:0000313|Proteomes:UP000199347};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00189};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00189}.
FT TRANSMEM 15..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 68..87
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 139..156
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 163..182
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
SQ SEQUENCE 199 AA; 22440 MW; AB9A4FC2CE4F18FA CRC64;
MSIFEREPGD PGRDHLPPLV KLLLELGPLV VFFFANARFD IFVATASFMV AIAISLGVSY
WLTKKLAIMP LVTGIVVLVF GTLTLILHDD VFIKMKPTIV NALFGTILLG GLAFNRSFLG
YVFDSVFRLD AEGWRKLTFR WGLFFFALAI LNEVVWRNFS TDFWVSFKVF GIMPLTIVFT
LTQMPLITRH SLEPLGGDK
//