ID A8ZXA3_DESOH Unreviewed; 403 AA.
AC A8ZXA3;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Mur ligase, middle domain protein {ECO:0000313|EMBL:ABW68482.1};
GN OrderedLocusNames=Dole_2679 {ECO:0000313|EMBL:ABW68482.1};
OS Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus
OS oleovorans).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW68482.1, ECO:0000313|Proteomes:UP000008561};
RN [1] {ECO:0000313|EMBL:ABW68482.1, ECO:0000313|Proteomes:UP000008561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3
RC {ECO:0000313|Proteomes:UP000008561};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the CapA family.
CC {ECO:0000256|ARBA:ARBA00005662}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000859; ABW68482.1; -; Genomic_DNA.
DR RefSeq; WP_012176093.1; NC_009943.1.
DR AlphaFoldDB; A8ZXA3; -.
DR STRING; 96561.Dole_2679; -.
DR KEGG; dol:Dole_2679; -.
DR eggNOG; COG2843; Bacteria.
DR HOGENOM; CLU_038823_2_2_7; -.
DR OrthoDB; 5405713at2; -.
DR Proteomes; UP000008561; Chromosome.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07381; MPP_CapA; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR019079; Capsule_synth_CapA.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR33393; POLYGLUTAMINE SYNTHESIS ACCESSORY PROTEIN RV0574C-RELATED; 1.
DR PANTHER; PTHR33393:SF11; POLYGLUTAMINE SYNTHESIS ACCESSORY PROTEIN RV0574C-RELATED; 1.
DR Pfam; PF09587; PGA_cap; 1.
DR SMART; SM00854; PGA_cap; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:ABW68482.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008561}.
FT DOMAIN 42..302
FT /note="Capsule synthesis protein CapA"
FT /evidence="ECO:0000259|SMART:SM00854"
SQ SEQUENCE 403 AA; 43993 MW; B5847D050FABE2D3 CRC64;
MTLKNRFTPY RLLLVVCVIT VGVYGCRAGD TADGLAHTGQ VHILFAGDTA FGESYQRVIA
QQAGEDILKT RGYDHGFAGL LPLLKRADTT VANLETPVTS LPASPLAGRK SYLHWSDIHA
APAALAKHNI KHLSLANNHT MDYGLQGLKQ TLDVLQQNGM ETFGAGASAA DGARPLALSY
KINGHPLRML VAAGFEYRPV YDRAFRFYAG KDKGGVNAWS IPRAAAQIRA LRGENPGAFI
IAFPHWGKNY QWKTTGQTAL AHALIDSGAD LVLGHGAHRL QEIELYHDRW IIYSLGNFVF
NAPGRYAEHD GPPFSLAALM AVTEEKGKFD CALSLYPVMS DNRITGYQPR FATKKEFDAL
YQSILDQSSD PGALKTRIAT GQDDVGPFIR LNVTPEPFLA KNV
//
