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Database: UniProt
Entry: C6M3N4_NEISI
LinkDB: C6M3N4_NEISI
Original site: C6M3N4_NEISI 
ID   C6M3N4_NEISI            Unreviewed;       194 AA.
AC   C6M3N4;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   SubName: Full=ErfK/YbiS/YcfS/YnhG {ECO:0000313|EMBL:EET45187.1};
GN   ORFNames=NEISICOT_01182 {ECO:0000313|EMBL:EET45187.1};
OS   Neisseria sicca ATCC 29256.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=547045 {ECO:0000313|EMBL:EET45187.1, ECO:0000313|Proteomes:UP000005365};
RN   [1] {ECO:0000313|EMBL:EET45187.1, ECO:0000313|Proteomes:UP000005365}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29256 {ECO:0000313|EMBL:EET45187.1,
RC   ECO:0000313|Proteomes:UP000005365};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00004752}.
CC   -!- SIMILARITY: Belongs to the YkuD family.
CC       {ECO:0000256|ARBA:ARBA00005992}.
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:EET45187.1}.
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DR   EMBL; ACKO02000005; EET45187.1; -; Genomic_DNA.
DR   RefSeq; WP_003757257.1; NZ_ACKO02000005.1.
DR   AlphaFoldDB; C6M3N4; -.
DR   eggNOG; COG3034; Bacteria.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000005365; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProt.
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; 2.40.440.10; L,D-transpeptidase catalytic domain-like; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   PANTHER; PTHR36699:SF1; L,D-TRANSPEPTIDASE YAFK-RELATED; 1.
DR   PANTHER; PTHR36699; LD-TRANSPEPTIDASE; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
PE   3: Inferred from homology;
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          58..192
FT                   /note="L,D-transpeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF03734"
FT   REGION          91..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   194 AA;  21140 MW;  379E11F65E8A679A CRC64;
     MKRGLKISLA AVLLLAVAAG VVWYSTPIRS EQTVATSGES SVAEPSETPL PENAVIDRLV
     VHKSKRTMSA YSQGKLLKTY PIALGKQPVG HKHFEGDGKT PEGKYRINDR NPNSAYHKNL
     GVSYPNEADK AYAAAQGKSP GGLIKIHGIK NGWGSIGKRH LQRDWTDGCI AVTDEEIDEL
     YRSVKHNAEI EILP
//
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