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Database: UniProt
Entry: A0A0P1ISH2_9RHOB
LinkDB: A0A0P1ISH2_9RHOB
Original site: A0A0P1ISH2_9RHOB 
ID   A0A0P1ISH2_9RHOB        Unreviewed;       203 AA.
AC   A0A0P1ISH2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=Inner membrane-spanning protein YciB {ECO:0000256|HAMAP-Rule:MF_00189};
GN   Name=yciB {ECO:0000256|HAMAP-Rule:MF_00189,
GN   ECO:0000313|EMBL:CUK26430.1};
GN   ORFNames=TA5114_02240 {ECO:0000313|EMBL:CUK26430.1};
OS   Cognatishimia activa.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cognatishimia.
OX   NCBI_TaxID=1715691 {ECO:0000313|EMBL:CUK26430.1, ECO:0000313|Proteomes:UP000051184};
RN   [1] {ECO:0000313|Proteomes:UP000051184}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5114 {ECO:0000313|Proteomes:UP000051184};
RA   Rodrigo-Torres Lidia, Arahal R.David.;
RL   Submitted (SEP-2015) 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; CYUE01000020; CUK26430.1; -; Genomic_DNA.
DR   RefSeq; WP_058315317.1; NZ_CYUE01000020.1.
DR   AlphaFoldDB; A0A0P1ISH2; -.
DR   STRING; 1715691.TA5113_01067; -.
DR   OrthoDB; 9788219at2; -.
DR   Proteomes; UP000051184; 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:UP000051184};
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..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT   TRANSMEM        74..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..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT   TRANSMEM        167..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
SQ   SEQUENCE   203 AA;  22755 MW;  44FA0AADE9B01D71 CRC64;
     MAGKPINPTL KMALELGPII LFFVGYLKFR DQSFLIGGTA YDGFILVTAA FVPLIALSSF
     ILWRLTGHLS KMQIATVVLV TVFGGLSVWL NDDRFFKMKP TMIYLLFGGV LGFGLLRGQS
     YLKFVMEEAL ALRNEGWMIL TKRLTAFFIG LAVLNEVIWR TQSTDTWVYF KTFGLTAAVF
     LFFMTQAGVL SRYAIEEEGE DAA
//
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