ID A0A5B8VJ90_9BACT Unreviewed; 446 AA.
AC A0A5B8VJ90;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Rod shape-determining protein RodA {ECO:0000313|EMBL:QEC71614.1};
GN ORFNames=FSB73_07980 {ECO:0000313|EMBL:QEC71614.1};
OS Arachidicoccus ginsenosidivorans.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Arachidicoccus.
OX NCBI_TaxID=496057 {ECO:0000313|EMBL:QEC71614.1, ECO:0000313|Proteomes:UP000321291};
RN [1] {ECO:0000313|EMBL:QEC71614.1, ECO:0000313|Proteomes:UP000321291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gsoil 809 {ECO:0000313|EMBL:QEC71614.1,
RC ECO:0000313|Proteomes:UP000321291};
RX PubMed=27974091; DOI=.1099/ijsem.0.001720;
RA Siddiqi M.Z., Aslam Z., Im W.T.;
RT "Arachidicoccus ginsenosidivorans sp. nov., with ginsenoside-converting
RT activity isolated from ginseng cultivating soil.";
RL Int. J. Syst. Evol. Microbiol. 67:1005-1010(2017).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP042434; QEC71614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B8VJ90; -.
DR KEGG; agi:FSB73_07980; -.
DR OrthoDB; 9768187at2; -.
DR Proteomes; UP000321291; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR InterPro; IPR018365; Cell_cycle_FtsW-rel_CS.
DR InterPro; IPR001182; FtsW/RodA.
DR NCBIfam; NF037961; RodA_shape; 1.
DR PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1.
DR PANTHER; PTHR30474:SF1; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE MRDB; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 1.
DR PROSITE; PS00428; FTSW_RODA_SPOVE; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000321291};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 145..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 349..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 383..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 416..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 446 AA; 49617 MW; 25A7079A1E1F2F1A CRC64;
MYQQEKLAKG IDWMVVFLYA ALVGIGILCI FMVEYNPDIN WASAFVSGQT EYSKQLIFAG
VCAILAIFIL LSDSKLYTAF ANLAYLFGIL LMLATFVLGK NINGSRSWIP LGGGFNLQPA
ELCKIFTSLA LAKYLSMQEL DFSKLRSQII ATIIAMLPAM ISILQNETGL ALVYCCFFIV
MFREGLPGAI LLIGFSFGVL VVATLIMDPD LLAIILTAIA IATIYLLRKK IKRSRRILAL
IIFVWAACVG IQRFAVPYIF NNILQCYQST RVYSMVGKVY DCSKNKSSMA REEENKTYAK
PDDYNVRQSK IAIGSGGIFG RGFLKGTQTR GKYVPEQQTD FVFTSIGEAF GFVGCAIFLL
TYLALLFRIV KIAERQRSVF SRVYAYCVAS IFLMHIAINV CMTVGLFPVV GIPLPLVSYG
GSSLVTFTIL IFIMLRLDAD RQMVLR
//
