ID G4SWE2_META2 Unreviewed; 551 AA.
AC G4SWE2;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=ErfK/YbiS/YcfS/YnhG family protein {ECO:0000313|EMBL:CCE24155.1};
GN OrderedLocusNames=MEALZ_2475 {ECO:0000313|EMBL:CCE24155.1};
OS Methylotuvimicrobium alcaliphilum (strain DSM 19304 / NCIMB 14124 / VKM
OS B-2133 / 20Z) (Methylomicrobium alcaliphilum).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylotuvimicrobium.
OX NCBI_TaxID=1091494 {ECO:0000313|EMBL:CCE24155.1, ECO:0000313|Proteomes:UP000008315};
RN [1] {ECO:0000313|Proteomes:UP000008315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19304 / NCIMB 14124 / VKM B-2133 / 20Z
RC {ECO:0000313|Proteomes:UP000008315};
RX PubMed=22207753; DOI=10.1128/JB.06392-11;
RA Vuilleumier S., Khmelenina V.N., Bringel F., Reshetnikov A.S., Lajus A.,
RA Mangenot S., Rouy Z., Op den Camp H.J., Jetten M.S., Dispirito A.A.,
RA Dunfield P., Klotz M.G., Semrau J.D., Stein L.Y., Barbe V., Medigue C.,
RA Trotsenko Y.A., Kalyuzhnaya M.G.;
RT "Genome sequence of the haloalkaliphilic methanotrophic bacterium
RT Methylomicrobium alcaliphilum 20Z.";
RL J. Bacteriol. 194:551-552(2012).
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: Belongs to the YkuD family.
CC {ECO:0000256|ARBA:ARBA00005992}.
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DR EMBL; FO082060; CCE24155.1; -; Genomic_DNA.
DR RefSeq; WP_014148931.1; NC_016112.1.
DR AlphaFoldDB; G4SWE2; -.
DR STRING; 1091494.MEALZ_2475; -.
DR KEGG; mah:MEALZ_2475; -.
DR PATRIC; fig|271065.3.peg.2547; -.
DR HOGENOM; CLU_020360_3_4_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000008315; Chromosome.
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 Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR005490; LD_TPept_cat_dom.
DR InterPro; IPR045380; LD_TPept_scaffold_dom.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR41533:SF2; BLR7131 PROTEIN; 1.
DR PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF20142; Scaffold; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000008315};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 60..203
FT /note="L,D-transpeptidase scaffold"
FT /evidence="ECO:0000259|Pfam:PF20142"
FT DOMAIN 231..288
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 316..485
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 551 AA; 62838 MW; F2061E95B031E8B7 CRC64;
MKQPLHKFLI AVTIIALFLP KMSTAEHLSV EESIRERIES AAEILDLSID NQPLNSQKGL
ISFYSDRQFS KAWLANGQPT PQAYQLMQIL NSADQHGLNK SNYHVTAINE RLERLKAPLN
ESEILILSVD LDLLLSDAFL TYGTHLLQGQ VNPQKLQSKW DTGRRATDMV KILSDAIDTN
SIEQSLNELM PKQPGYRSLV RALADYRAIK DRGGWPSVTE GPSLRPNEKN PRIIELRKRL
VASGDLANDV ALDNIEFDQS LQQAVKYFQK RHGLETDSIV GRATLEALNV SVDHRIAQIR
ANLERWRWLP EDLGARHIMV NIAGFALDFV GNGEVLLHMP VIVGKTYRET PIFTGSMTYL
VINPSWYVPN SIAVKDKLPI LARDPYYIER NHMKLYRGWG ANRTEINPLS VNWRQVNPNN
FPFRLVQKPG PKNAMGKVKF MFPNPHNVYL HDTSEPSLFN RVDRTFSSGC IRVGKPFALA
NLVLENNSRM TPDAIREAFD QSDQKTVTLL NPIPVHILYW TAWVDLEGVV QFRRDIYNRD
DELIQKLQKS F
//
