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Database: UniProt
Entry: A0A0F4RF84_9RHOB
LinkDB: A0A0F4RF84_9RHOB
Original site: A0A0F4RF84_9RHOB 
ID   A0A0F4RF84_9RHOB        Unreviewed;       272 AA.
AC   A0A0F4RF84;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Cell division coordinator CpoB {ECO:0000256|HAMAP-Rule:MF_02066};
DE   Flags: Precursor;
GN   Name=cpoB {ECO:0000256|HAMAP-Rule:MF_02066};
GN   ORFNames=TW80_15170 {ECO:0000313|EMBL:KJZ18274.1};
OS   Loktanella sp. S4079.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Loktanella.
OX   NCBI_TaxID=579483 {ECO:0000313|EMBL:KJZ18274.1, ECO:0000313|Proteomes:UP000033741};
RN   [1] {ECO:0000313|EMBL:KJZ18274.1, ECO:0000313|Proteomes:UP000033741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S4079 {ECO:0000313|EMBL:KJZ18274.1,
RC   ECO:0000313|Proteomes:UP000033741};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
CC   -!- FUNCTION: Mediates coordination of peptidoglycan synthesis and outer
CC       membrane constriction during cell division. {ECO:0000256|HAMAP-
CC       Rule:MF_02066}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_02066}.
CC   -!- SIMILARITY: Belongs to the CpoB family. {ECO:0000256|HAMAP-
CC       Rule:MF_02066}.
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:KJZ18274.1}.
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DR   EMBL; JXYE01000007; KJZ18274.1; -; Genomic_DNA.
DR   RefSeq; WP_045998302.1; NZ_JXYE01000007.1.
DR   AlphaFoldDB; A0A0F4RF84; -.
DR   STRING; 579483.TW80_15170; -.
DR   PATRIC; fig|579483.3.peg.3119; -.
DR   OrthoDB; 9763909at2; -.
DR   Proteomes; UP000033741; Unassembled WGS sequence.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:UniProtKB-UniRule.
DR   GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   HAMAP; MF_02066; CpoB; 1.
DR   InterPro; IPR034706; CpoB.
DR   InterPro; IPR014162; CpoB_C.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   NCBIfam; TIGR02795; tol_pal_ybgF; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF13174; TPR_6; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Cell division {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Coiled coil {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Periplasm {ECO:0000256|HAMAP-Rule:MF_02066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033741};
KW   Signal {ECO:0000256|HAMAP-Rule:MF_02066}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT   CHAIN           21..272
FT                   /note="Cell division coordinator CpoB"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
FT                   /id="PRO_5009983622"
FT   COILED          25..85
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02066"
SQ   SEQUENCE   272 AA;  29023 MW;  A6D873E237E9E882 CRC64;
     MLHRIAVVLS LLLMPVSAVA QEETLADIRQ QLTALYVDIQ RLHRELSTTG GVSNGVSGNT
     LLDRVNAIEA ELQRLTSKTE QLEFRVNRIT VDGTNRIGDL EFRLCELEAQ CDIAQLGDTP
     SLGGVDNGAD VPAPNLPPAT GGPSLAIGEK TDFERAQEAL ANRDFRGAVD QLETFNASYP
     GSPLAAQASY MRGEALEGLD QPTAAARAYL ESFSGDPEGE QAPRALYKLG ASLGTIGQTQ
     DACLTLAEVN VRFPTSPVVN DAQLAMQNLG CQ
//
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