ID A0A2A5B346_9RICK Unreviewed; 179 AA.
AC A0A2A5B346;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Inner membrane-spanning protein YciB {ECO:0000256|HAMAP-Rule:MF_00189};
GN Name=ispZ {ECO:0000313|EMBL:PCJ25953.1};
GN Synonyms=yciB {ECO:0000256|HAMAP-Rule:MF_00189};
GN ORFNames=COA94_05710 {ECO:0000313|EMBL:PCJ25953.1};
OS Rickettsiales bacterium.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=2026788 {ECO:0000313|EMBL:PCJ25953.1, ECO:0000313|Proteomes:UP000218523};
RN [1] {ECO:0000313|Proteomes:UP000218523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT "A dynamic microbial community with high functional redundancy inhabits the
RT cold, oxic subseafloor aquifer.";
RL Submitted (AUG-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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00189}.
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:PCJ25953.1}.
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DR EMBL; NVVL01000053; PCJ25953.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A5B346; -.
DR Proteomes; UP000218523; 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 Transmembrane {ECO:0000256|HAMAP-Rule:MF_00189};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00189}.
FT TRANSMEM 26..44
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 51..74
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 80..97
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
FT TRANSMEM 146..165
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00189"
SQ SEQUENCE 179 AA; 20726 MW; A93A69443085F6F0 CRC64;
MVKFLSEFAP LIAFFYGYKT GGILEATLYM VVVSVIGIVV TYIVERRINK VNLVTTALLL
VSASLTLFSG NSIFIKMKPT VLYCLFALAL FVTHFKWRPA IQYALGAAIK FKDQRAWYHL
NKRFMFFFLL MAAANETIWR NFSEDIWVNF KVFGALPITI IFIMMQVPFI MKHKIDEEH
//