ID C3M9I0_SINFN Unreviewed; 442 AA.
AC C3M9I0;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Amidase {ECO:0000313|EMBL:ACP24746.1};
GN OrderedLocusNames=NGR_c09560 {ECO:0000313|EMBL:ACP24746.1};
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24746.1, ECO:0000313|Proteomes:UP000001054};
RN [1] {ECO:0000313|EMBL:ACP24746.1, ECO:0000313|Proteomes:UP000001054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP24746.1; -; Genomic_DNA.
DR RefSeq; WP_012707530.1; NC_012587.1.
DR RefSeq; YP_002825499.1; NC_012587.1.
DR AlphaFoldDB; C3M9I0; -.
DR STRING; 394.NGR_c09560; -.
DR KEGG; rhi:NGR_c09560; -.
DR PATRIC; fig|394.7.peg.3777; -.
DR eggNOG; COG2989; Bacteria.
DR HOGENOM; CLU_020360_5_2_5; -.
DR OrthoDB; 9778545at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001054; 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; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR038063; Transpep_catalytic_dom.
DR PANTHER; PTHR41533; L,D-TRANSPEPTIDASE HI_1667-RELATED; 1.
DR PANTHER; PTHR41533:SF1; L,D-TRANSPEPTIDASE YCBB-RELATED; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR Pfam; PF03734; YkuD; 1.
DR SUPFAM; SSF141523; L,D-transpeptidase catalytic domain-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..442
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002927681"
FT DOMAIN 111..162
FT /note="Peptidoglycan binding-like"
FT /evidence="ECO:0000259|Pfam:PF01471"
FT DOMAIN 196..363
FT /note="L,D-transpeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF03734"
SQ SEQUENCE 442 AA; 48740 MW; DBEB66AE912EFD04 CRC64;
MSKNNGIDAF SRRAFLRSAA TFGAAAWAGA ASAQDALGEL INSPRRGSWD DQFDAKASRT
ATAVLSNTPV FGPQTIGHVQ QAIFDYQQIV AAGGWPQVPQ TGARLELGVT DPSVQQLRQR
LMVSGDLPRS AGISSSFDSY VDGAVKRFQA RHGLPADGVI GEYSFKALNV DAATRLAQLE
TNLVRLQSMS GDLGRRYVMV NIPAAYIEAV ENGRVVLRHT AIVGKIDRQS PILNSKIYEV
ILNPYWTAPR SIVQKDIMPL MRKDPTYLER NAIRLLDGSG NEVSPETVDW NAEKAPNLMF
RQDPGKINAM SSTKINFHNE HSVYMHDTPQ QGLFNKLMRF ESSGCVRVQN VRDLSTWLLK
ETPGWSRQQI EATIKTGVNT PIKLAEEVPV YFTYITAWSA KDRVVQFRDD IYQRDGAAEL
ALQTTTGIEQ SPGAIDADAL PQ
//