ID A0A1I7N5J1_9BACT Unreviewed; 432 AA.
AC A0A1I7N5J1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Rod shape determining protein RodA {ECO:0000313|EMBL:SFV29920.1};
GN ORFNames=SAMN05660895_0657 {ECO:0000313|EMBL:SFV29920.1};
OS Thermoflavifilum thermophilum.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Thermoflavifilum.
OX NCBI_TaxID=1393122 {ECO:0000313|EMBL:SFV29920.1, ECO:0000313|Proteomes:UP000199537};
RN [1] {ECO:0000313|Proteomes:UP000199537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14807 {ECO:0000313|Proteomes:UP000199537};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FPCJ01000001; SFV29920.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7N5J1; -.
DR STRING; 1393122.SAMN05660895_0657; -.
DR Proteomes; UP000199537; Unassembled WGS sequence.
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 InterPro; IPR011923; RodA/MrdB.
DR NCBIfam; NF037961; RodA_shape; 1.
DR NCBIfam; TIGR02210; rodA_shape; 1.
DR PANTHER; PTHR30474; CELL CYCLE PROTEIN; 1.
DR PANTHER; PTHR30474:SF1; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE MRDB; 1.
DR Pfam; PF01098; FTSW_RODA_SPOVE; 2.
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:UP000199537};
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 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 149..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 215..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..264
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..357
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 369..396
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 402..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 432 AA; 48507 MW; C38250EA30E23EF2 CRC64;
MDTHVRTSTD LIKPGIDRVL MALYFILVLI GLFSIFAVEH RPGEDVWYNV LHLSKNYSRQ
LMWVCISLVL ALGILLVDSK LFPALANLMY VFGILLLLLV LVAGKDIKGS HSWLVIGGFQ
FQPAEFTKLT TNLALAKYLS RLDVDFSTLR ARLIAIGLIL LPAAIIVMQS ETGLALVYLS
FFLVLYREGL PGIILIVGFS VIVLVLSALL VEKHILLMIF SVAAAFVIYF MRRSFRRHPE
RLFLILLIWG FCSVFVMQVV PYIFTHVLKP YQVSRINVML GKEVSPKSSY NVLQSKIAIG
SGGLFGKGYL KGTQTRYEFV PEQSTDFIFC TIGEDFGFIG SIGLLGLYLI LLFRIIQVAE
RQRSTFSRVY AYGLASILFF HVAINIGMTT GLAPVIGIPL PWMSYGGSSM ITFTMMLFIL
IRLDADRQKI LR
//
