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Database: UniProt
Entry: A0A1X7NSB8_9RHOB
LinkDB: A0A1X7NSB8_9RHOB
Original site: A0A1X7NSB8_9RHOB 
ID   A0A1X7NSB8_9RHOB        Unreviewed;       202 AA.
AC   A0A1X7NSB8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=SAMN05661107_1057 {ECO:0000313|EMBL:SMH40234.1};
OS   Maritimibacter sp. HL-12.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=1162418 {ECO:0000313|EMBL:SMH40234.1, ECO:0000313|Proteomes:UP000193836};
RN   [1] {ECO:0000313|EMBL:SMH40234.1, ECO:0000313|Proteomes:UP000193836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-12 {ECO:0000313|EMBL:SMH40234.1,
RC   ECO:0000313|Proteomes:UP000193836};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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}.
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DR   EMBL; FXBQ01000001; SMH40234.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7NSB8; -.
DR   STRING; 1162418.SAMN05661107_1057; -.
DR   OrthoDB; 9788219at2; -.
DR   Proteomes; UP000193836; Unassembled WGS sequence.
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.
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:UP000193836};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00189};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00189}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT   TRANSMEM        41..61
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT   TRANSMEM        73..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT   TRANSMEM        143..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT   TRANSMEM        166..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
SQ   SEQUENCE   202 AA;  22700 MW;  419DE03EB902B2DB CRC64;
     MTDKALKPAV KIGLEYGPII AFFIGYMLLR DRVFTVGGTE YSGFVAVTAM FIPLLAVATF
     LQWRLSGHLS KMQIATLVIV IAFGGLSVWL NDERFFKMKP TIIYLLFAGI LGFGLLRGQS
     YLQTVMDQAM PLTREGWMIL TRRLAAFFFA LALANEAVWR TMSTDAWVSF KTFGLPIAIF
     AFFMLQSGVF SRHGTDEEHK DV
//
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