ID   CBXPD_MYCTU             Reviewed;         461 AA.
AC   O06380; F2GEZ8; I6YGT2;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Carboxypeptidase Rv3627c {ECO:0000305};
DE            EC=3.4.16.- {ECO:0000269|PubMed:31000162};
DE   Flags: Precursor;
GN   OrderedLocusNames=Rv3627c {ECO:0000312|EMBL:CCP46450.1};
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2] {ECO:0007744|PubMed:21969609}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [3]
RP   FUNCTION, AND OVEREXPRESSION.
RC   STRAIN=H37Rv;
RX   PubMed=31000162; DOI=10.1016/j.enzmictec.2019.03.003;
RA   Zhang W., Li S., Ma L., Ding W., Xu Y.;
RT   "Identification of a novel carboxypeptidase encoded by Rv3627c that plays a
RT   potential role in mycobacteria morphology and cell division.";
RL   Enzyme Microb. Technol. 126:32-40(2019).
CC   -!- FUNCTION: Carboxypeptidase that cleaves terminal D-alanine from
CC       peptidoglycan in the mycobacterial cell wall. May cleave L-Lys-D-Ala
CC       and/or D-Ala-D-Ala peptide bonds. Exerts important effects on
CC       mycobacterial cell morphology and cell division.
CC       {ECO:0000269|PubMed:31000162}.
CC   -!- MISCELLANEOUS: Overexpression in M. smegmatis leads to elongated cells
CC       and promotes the formation of increased numbers of Z-rings.
CC       {ECO:0000269|PubMed:31000162}.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP46450.1; -; Genomic_DNA.
DR   RefSeq; NP_218144.1; NC_000962.3.
DR   RefSeq; WP_003899610.1; NZ_NVQJ01000045.1.
DR   AlphaFoldDB; O06380; -.
DR   SMR; O06380; -.
DR   STRING; 83332.Rv3627c; -.
DR   MEROPS; S13.004; -.
DR   PaxDb; O06380; -.
DR   DNASU; 885728; -.
DR   GeneID; 885728; -.
DR   KEGG; mtu:Rv3627c; -.
DR   PATRIC; fig|83332.111.peg.4033; -.
DR   TubercuList; Rv3627c; -.
DR   eggNOG; COG2027; Bacteria.
DR   InParanoid; O06380; -.
DR   OMA; HSDNTLA; -.
DR   PhylomeDB; O06380; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 2.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   PANTHER; PTHR30023; PTHR30023; 2.
DR   Pfam; PF02113; Peptidase_S13; 2.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   TIGRFAMs; TIGR00666; PBP4; 2.
PE   1: Evidence at protein level;
KW   Carboxypeptidase; Cell wall biogenesis/degradation; Hydrolase; Protease;
KW   Reference proteome; Signal.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..461
FT                   /note="Carboxypeptidase Rv3627c"
FT                   /id="PRO_5004156985"
FT   ACT_SITE        114
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P39844"
FT   ACT_SITE        117
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P39844"
FT   ACT_SITE        295
FT                   /evidence="ECO:0000250|UniProtKB:P39844"
SQ   SEQUENCE   461 AA;  46834 MW;  9EFF96CCB75E4997 CRC64;
     MGPTRWRKST HVVVGAAVLA FVAVVVAAAA LVTTGGHRAG VRAPAPPPRP PTVKAGVVPV
     ADTAATPSAA GVTAALAVVA ADPDLGKLAG RITDALTGQE LWQRLDDVPL VPASTNKILT
     AAAALLTLDR QARISTRVVA GGQNPQGPVV LVGAGDPTLS AAPPGQDTWY HGAARIGDLV
     EQIRRSGVTP TAVQVDASAF SGPTMAPGWD PADIDNGDIA PIEAAMIDAG RIQPTTVNSR
     RSRTPALDAG RELAKALGLD PAAVTIASAP AGARQLAVVQ SAPLIQRLSQ MMNASDNVMA
     ECIGREVAVA INRPQSFSGA VDAVTSRLNT AHIDTAGAAL VDSSGLSLDN RLTARTLDAT
     MQAAAGPDQP ALRPLLDLLP IAGGSGTLGE RFLDAATDQG PAGWLRAKTG SLTAINSLVG
     VLTDRSGRVL TFAFISNEAG PNGRNAMDAL ATKLWFCGCT T