ID I3UB46_ADVKW Unreviewed; 194 AA.
AC I3UB46;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Inner membrane-spanning protein YciB {ECO:0000256|HAMAP-Rule:MF_00189};
GN Name=yciB {ECO:0000256|HAMAP-Rule:MF_00189};
GN OrderedLocusNames=TKWG_09605 {ECO:0000313|EMBL:AFK62234.1};
OS Advenella kashmirensis (strain DSM 17095 / LMG 22695 / WT001)
OS (Tetrathiobacter kashmirensis).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae.
OX NCBI_TaxID=1036672 {ECO:0000313|EMBL:AFK62234.1, ECO:0000313|Proteomes:UP000005267};
RN [1] {ECO:0000313|EMBL:AFK62234.1, ECO:0000313|Proteomes:UP000005267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17095 / LMG 22695 / WT001
RC {ECO:0000313|Proteomes:UP000005267};
RX PubMed=21914874; DOI=10.1128/JB.05781-11;
RA Ghosh W., George A., Agarwal A., Raj P., Alam M., Pyne P., Das Gupta S.K.;
RT "Whole-genome shotgun sequencing of the sulfur-oxidizing chemoautotroph
RT Tetrathiobacter kashmirensis.";
RL J. Bacteriol. 193:5553-5554(2011).
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}.
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DR EMBL; CP003555; AFK62234.1; -; Genomic_DNA.
DR RefSeq; WP_014750325.1; NC_017964.1.
DR AlphaFoldDB; I3UB46; -.
DR STRING; 1036672.TKWG_09605; -.
DR KEGG; aka:TKWG_09605; -.
DR HOGENOM; CLU_089554_2_0_4; -.
DR OrthoDB; 9788219at2; -.
DR Proteomes; UP000005267; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR HAMAP; MF_00189; YciB; 1.
DR InterPro; IPR006008; YciB.
DR PANTHER; PTHR36917:SF1; INNER MEMBRANE-SPANNING PROTEIN YCIB; 1.
DR PANTHER; PTHR36917; INTRACELLULAR SEPTATION PROTEIN A-RELATED; 1.
DR Pfam; PF04279; IspA; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Transmembrane {ECO:0000256|HAMAP-Rule:MF_00189};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00189}.
FT TRANSMEM 12..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 53..70
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 82..102
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 123..144
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 150..172
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
SQ SEQUENCE 194 AA; 22200 MW; 98D5620D3FE4C4C8 CRC64;
MKKLLFDFFP LVLFFVAFKV ADIYVATWVA IACSVLQILW LKLRGRPIEA TNWMNVIIIV
VFGGATIYFH NDTFVKWKPT VLYWMFALIL LGARLLMNKN VLRKMLATQM RLPDRIWDRL
SDTWAGFFLF AGALNLVVAF SGYFTLEQWA AFKAFGMTIL LVIFAIGQSV WLGRHMQEVP
ATPGPVALPE KTND
//