ID A5D241_PELTS Unreviewed; 412 AA.
AC A5D241;
DT 12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 12-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Uncharacterized protein conserved in bacteria {ECO:0000313|EMBL:BAF59677.1};
GN Name=ErfK {ECO:0000313|EMBL:BAF59677.1};
GN OrderedLocusNames=PTH_1496 {ECO:0000313|EMBL:BAF59677.1};
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF59677.1, ECO:0000313|Proteomes:UP000006556};
RN [1] {ECO:0000313|Proteomes:UP000006556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556};
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
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DR EMBL; AP009389; BAF59677.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D241; -.
DR KEGG; pth:PTH_1496; -.
DR eggNOG; COG1376; Bacteria.
DR HOGENOM; CLU_668556_0_0_9; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000006556; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd16913; YkuD_like; 1.
DR Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 2.
DR Gene3D; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR036582; Mao_N_sf.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR30582; L,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30582:SF4; L,D-TRANSPEPTIDASE YQJB-RELATED; 1.
DR Pfam; PF07833; Cu_amine_oxidN1; 2.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 2.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006556};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..412
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002680802"
FT DOMAIN 28..155
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
FT DOMAIN 191..280
FT /note="Copper amine oxidase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07833"
FT DOMAIN 319..408
FT /note="Copper amine oxidase-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF07833"
SQ SEQUENCE 412 AA; 44773 MW; 2299D067E5ECAD49 CRC64;
MLIRFVFIMP VLCLALLSAC RQPAEAAPRI VINKGTNQLA FFEDGFLMDV FPVATGRQPH
FTPEGVWQVV VKLVYPSWRP PGGGPVVPGG APENPLGPRW LGLDALGTNG SSYGLHGNND
PPSIGTYATS GCVRMHNQDI LWLYDRVPVG TEVEIINSGE DLTGWKKFSR ITVNGAEPEF
LPHLGPVQAG ETTYLPVRPV AAALGYRLWW DESAGTLLAA NIEREVFLAP GSRLVTVNNC
SFTAEEAPFL LENTTCVPDY YFERFFGAKI YRDEENNTLK LEAPVDKAAG RLVKYHLELK
VNGKTVILPE ELTPLTDGEN LLLPARPFCS AAGASVSWNG QTRSVEIEMK GRHASIPVNG
SPALVNGTAV ATASNIFTRN GSSYVSLRFL ADVFGFQAET GGKARTLSVY TF
//
