ID A0A073K1A7_9BACI Unreviewed; 611 AA.
AC A0A073K1A7;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Polysaccharide biosynthesis protein EpsC {ECO:0000313|EMBL:KEK20275.1};
GN ORFNames=BAMA_17715 {ECO:0000313|EMBL:KEK20275.1};
OS Bacillus manliponensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=574376 {ECO:0000313|EMBL:KEK20275.1, ECO:0000313|Proteomes:UP000027822};
RN [1] {ECO:0000313|EMBL:KEK20275.1, ECO:0000313|Proteomes:UP000027822}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 15802 {ECO:0000313|EMBL:KEK20275.1,
RC ECO:0000313|Proteomes:UP000027822};
RA Lai Q., Liu Y., Shao Z.;
RT "Draft genome sequence of Bacillus manliponensis JCM 15802 (MCCC
RT 1A00708).";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the polysaccharide synthase family.
CC {ECO:0000256|ARBA:ARBA00007430}.
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:KEK20275.1}.
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DR EMBL; JOTN01000004; KEK20275.1; -; Genomic_DNA.
DR RefSeq; WP_034637667.1; NZ_JOTN01000004.1.
DR AlphaFoldDB; A0A073K1A7; -.
DR STRING; 574376.BAMA_17715; -.
DR eggNOG; COG1086; Bacteria.
DR OrthoDB; 9803111at2; -.
DR Proteomes; UP000027822; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd05237; UDP_invert_4-6DH_SDR_e; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR003869; Polysac_CapD-like.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR43318:SF1; POLYSACCHARIDE BIOSYNTHESIS PROTEIN EPSC-RELATED; 1.
DR PANTHER; PTHR43318; UDP-N-ACETYLGLUCOSAMINE 4,6-DEHYDRATASE; 1.
DR Pfam; PF13727; CoA_binding_3; 1.
DR Pfam; PF02719; Polysacc_synt_2; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027822};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 35..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 278..561
FT /note="Polysaccharide biosynthesis protein CapD-like"
FT /evidence="ECO:0000259|Pfam:PF02719"
SQ SEQUENCE 611 AA; 68767 MW; 32127F9E76C3174A CRC64;
MTYQQRISLL LIIDSVIVLS AIFFSSFFVN ASFHVIAFSS VMSSITLLVS HHFFAFIYKL
YKKAWEYASV GELLIIFKAV TLSIVTTAIL QQAVLQEVYF RLLLVTWMMH ILLIGGSRFL
WRLMRDSYFQ KKSTKKRALI IGAGSAGTMV VRQLLHNNEA ELLPVAFIDD NVKKHKLHIL
GVPVVGGVKE IESIVERLRI ESIIIAIPSL GKKELNEIFK ECSNTKVKTQ ILPMLEDLVT
GKVSVNEFRD VQVEDLLGRE PVELDINSIS EYVKDKVVLV TGAGGSIGSE ICRQVAIFQP
RQLILLGHGE NSIYSIHMEL KESYGDMKTI FIPEIADIQD ERKILSIMHQ YRPHVVYHAA
AHKHVPLMEY NPEEAVKNNV VGTMNVAKAA KKYDVDTFVM VSSDKAVNPT SVMGATKRLA
EMIVQQQDKG SHTKFVAVRF GNVLGSRGSV IPLFKKQIQK GGPVTVTHPE MIRYFMTIRE
ASKLVIQAGS LAKGGEIFVL DMGEPVKIVD LAKNLIKLSG NSIDEIGIEF TGMRPGEKLF
EELLTDDEVH EEQIHPRIYI GKETNIYIEE IENILSIYEE LNKEELRNKL LYVANNDKLP
KPLLPTYVNG N
//
